The non-gastric H,K-ATPase as a tool to study the ouabain-binding site in Na,K-ATPase

Abstract Based on studies with chimeras between (non-)gastric H,K-ATPase and Na,K-ATPase, a model for the ouabain binding site has recently been presented (Qiu et al. J.Biol.Chem. 280 (2005) 32349). In this model, hydrogen bonds between specific amino acid residues of Na,K-ATPase and hydroxyl groups...
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Autor*in:	De Pont, Jan Joep H. H. M. [verfasserIn] Swarts, Herman G. P. [verfasserIn] Karawajczyk, Anna [verfasserIn] Schaftenaar, Gijs [verfasserIn] Willems, Peter H. G. M. [verfasserIn] Koenderink, Jan B. [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2008

Schlagwörter:	Non-gastric H,K-ATPase Na,K-ATPase Ouabain Strophanthidin Digoxin

Übergeordnetes Werk:	Enthalten in: Pflügers Archiv - Berlin : Springer, 1868, 457(2008), 3 vom: 07. März, Seite 623-634
Übergeordnetes Werk:	volume:457 ; year:2008 ; number:3 ; day:07 ; month:03 ; pages:623-634

Links:	Volltext

DOI / URN:	10.1007/s00424-008-0467-8

Katalog-ID:	SPR005611555

Internformat


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100	1		\|a De Pont, Jan Joep H. H. M. \|e verfasserin \|4 aut
245	1	4	\|a The non-gastric H,K-ATPase as a tool to study the ouabain-binding site in Na,K-ATPase
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520			\|a Abstract Based on studies with chimeras between (non-)gastric H,K-ATPase and Na,K-ATPase, a model for the ouabain binding site has recently been presented (Qiu et al. J.Biol.Chem. 280 (2005) 32349). In this model, hydrogen bonds between specific amino acid residues of Na,K-ATPase and hydroxyl groups of ouabain play a crucial role. In the present study, a series of ouabain analogues were tested on baculovirus-expressed Na,K-ATPase and an ouabain-sensitive mutant of non-gastric H,K-ATPase (D312E/ S319G/ A778P/ I795L/ F802C). For each analogue, the results obtained by measuring ATPase inhibition and [3H]ouabain replacement agreed rather well. In Na,K-ATPase, strophanthidin had a 7–10 times higher and digoxin a 4–12 times lower affinity than ouabain. The results of the non-gastric H,K-ATPase mutant were rather similar to that of Na,K-ATPase with exception of dihydro-ouabain that showed a much lower affinity with the non-gastric H,K-ATPase mutant. Docking studies showed that all analogues bind to the same pocket in Na,K-ATPase. However, the amino acids to which hydrogen bonds were formed differed and depended on the availability of hydroxyl or keto groups in the ouabain analogues.
650		4	\|a Non-gastric H,K-ATPase \|7 (dpeaa)DE-He213
650		4	\|a Na,K-ATPase \|7 (dpeaa)DE-He213
650		4	\|a Ouabain \|7 (dpeaa)DE-He213
650		4	\|a Strophanthidin \|7 (dpeaa)DE-He213
650		4	\|a Digoxin \|7 (dpeaa)DE-He213
700	1		\|a Swarts, Herman G. P. \|e verfasserin \|4 aut
700	1		\|a Karawajczyk, Anna \|e verfasserin \|4 aut
700	1		\|a Schaftenaar, Gijs \|e verfasserin \|4 aut
700	1		\|a Willems, Peter H. G. M. \|e verfasserin \|4 aut
700	1		\|a Koenderink, Jan B. \|e verfasserin \|4 aut
773	0	8	\|i Enthalten in \|t Pflügers Archiv \|d Berlin : Springer, 1868 \|g 457(2008), 3 vom: 07. März, Seite 623-634 \|w (DE-627)25463897X \|w (DE-600)1463014-X \|x 1432-2013 \|7 nnns
773	1	8	\|g volume:457 \|g year:2008 \|g number:3 \|g day:07 \|g month:03 \|g pages:623-634
856	4	0	\|u https://dx.doi.org/10.1007/s00424-008-0467-8 \|z kostenfrei \|3 Volltext
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912			\|a GBV_ILN_20
912			\|a GBV_ILN_22
912			\|a GBV_ILN_23
912			\|a GBV_ILN_24
912			\|a GBV_ILN_31
912			\|a GBV_ILN_32
912			\|a GBV_ILN_39
912			\|a GBV_ILN_40
912			\|a GBV_ILN_60
912			\|a GBV_ILN_62
912			\|a GBV_ILN_63
912			\|a GBV_ILN_65
912			\|a GBV_ILN_69
912			\|a GBV_ILN_70
912			\|a GBV_ILN_73
912			\|a GBV_ILN_74
912			\|a GBV_ILN_90
912			\|a GBV_ILN_95
912			\|a GBV_ILN_100
912			\|a GBV_ILN_101
912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
912			\|a GBV_ILN_120
912			\|a GBV_ILN_138
912			\|a GBV_ILN_150
912			\|a GBV_ILN_151
912			\|a GBV_ILN_152
912			\|a GBV_ILN_161
912			\|a GBV_ILN_170
912			\|a GBV_ILN_171
912			\|a GBV_ILN_187
912			\|a GBV_ILN_213
912			\|a GBV_ILN_224
912			\|a GBV_ILN_230
912			\|a GBV_ILN_250
912			\|a GBV_ILN_267
912			\|a GBV_ILN_281
912			\|a GBV_ILN_285
912			\|a GBV_ILN_293
912			\|a GBV_ILN_370
912			\|a GBV_ILN_602
912			\|a GBV_ILN_636
912			\|a GBV_ILN_702
912			\|a GBV_ILN_2001
912			\|a GBV_ILN_2003
912			\|a GBV_ILN_2004
912			\|a GBV_ILN_2005
912			\|a GBV_ILN_2006
912			\|a GBV_ILN_2007
912			\|a GBV_ILN_2008
912			\|a GBV_ILN_2009
912			\|a GBV_ILN_2010
912			\|a GBV_ILN_2011
912			\|a GBV_ILN_2014
912			\|a GBV_ILN_2015
912			\|a GBV_ILN_2020
912			\|a GBV_ILN_2021
912			\|a GBV_ILN_2025
912			\|a GBV_ILN_2026
912			\|a GBV_ILN_2027
912			\|a GBV_ILN_2031
912			\|a GBV_ILN_2034
912			\|a GBV_ILN_2037
912			\|a GBV_ILN_2038
912			\|a GBV_ILN_2039
912			\|a GBV_ILN_2044
912			\|a GBV_ILN_2048
912			\|a GBV_ILN_2049
912			\|a GBV_ILN_2050
912			\|a GBV_ILN_2055
912			\|a GBV_ILN_2057
912			\|a GBV_ILN_2059
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2064
912			\|a GBV_ILN_2065
912			\|a GBV_ILN_2068
912			\|a GBV_ILN_2070
912			\|a GBV_ILN_2086
912			\|a GBV_ILN_2088
912			\|a GBV_ILN_2093
912			\|a GBV_ILN_2106
912			\|a GBV_ILN_2107
912			\|a GBV_ILN_2108
912			\|a GBV_ILN_2110
912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2112
912			\|a GBV_ILN_2113
912			\|a GBV_ILN_2116
912			\|a GBV_ILN_2118
912			\|a GBV_ILN_2119
912			\|a GBV_ILN_2122
912			\|a GBV_ILN_2129
912			\|a GBV_ILN_2143
912			\|a GBV_ILN_2144
912			\|a GBV_ILN_2147
912			\|a GBV_ILN_2148
912			\|a GBV_ILN_2152
912			\|a GBV_ILN_2153
912			\|a GBV_ILN_2188
912			\|a GBV_ILN_2190
912			\|a GBV_ILN_2232
912			\|a GBV_ILN_2336
912			\|a GBV_ILN_2446
912			\|a GBV_ILN_2470
912			\|a GBV_ILN_2472
912			\|a GBV_ILN_2507
912			\|a GBV_ILN_2522
912			\|a GBV_ILN_2548
912			\|a GBV_ILN_4012
912			\|a GBV_ILN_4035
912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4046
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4126
912			\|a GBV_ILN_4242
912			\|a GBV_ILN_4246
912			\|a GBV_ILN_4249
912			\|a GBV_ILN_4251
912			\|a GBV_ILN_4305
912			\|a GBV_ILN_4306
912			\|a GBV_ILN_4307
912			\|a GBV_ILN_4313
912			\|a GBV_ILN_4322
912			\|a GBV_ILN_4323
912			\|a GBV_ILN_4324
912			\|a GBV_ILN_4325
912			\|a GBV_ILN_4326
912			\|a GBV_ILN_4328
912			\|a GBV_ILN_4333
912			\|a GBV_ILN_4334
912			\|a GBV_ILN_4335
912			\|a GBV_ILN_4336
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4393
912			\|a GBV_ILN_4700
936	b	k	\|a 42.63 \|q ASE
936	b	k	\|a 44.37 \|q ASE
951			\|a AR
952			\|d 457 \|j 2008 \|e 3 \|b 07 \|c 03 \|h 623-634

Indexfelder

author_variant	p j j h h m d pjjhhm pjjhhmd h g p s hgp hgps a k ak g s gs p h g m w phgm phgmw j b k jb jbk
matchkey_str	article:14322013:2008----::hnnatihapsaaolotdteubibn
hierarchy_sort_str	2008
bklnumber	42.63 44.37
publishDate	2008
allfields	10.1007/s00424-008-0467-8 doi (DE-627)SPR005611555 (SPR)s00424-008-0467-8-e DE-627 ger DE-627 rakwb eng 610 ASE 610 590 ASE 42.63 bkl 44.37 bkl De Pont, Jan Joep H. H. M. verfasserin aut The non-gastric H,K-ATPase as a tool to study the ouabain-binding site in Na,K-ATPase 2008 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Based on studies with chimeras between (non-)gastric H,K-ATPase and Na,K-ATPase, a model for the ouabain binding site has recently been presented (Qiu et al. J.Biol.Chem. 280 (2005) 32349). In this model, hydrogen bonds between specific amino acid residues of Na,K-ATPase and hydroxyl groups of ouabain play a crucial role. In the present study, a series of ouabain analogues were tested on baculovirus-expressed Na,K-ATPase and an ouabain-sensitive mutant of non-gastric H,K-ATPase (D312E/ S319G/ A778P/ I795L/ F802C). For each analogue, the results obtained by measuring ATPase inhibition and [3H]ouabain replacement agreed rather well. In Na,K-ATPase, strophanthidin had a 7–10 times higher and digoxin a 4–12 times lower affinity than ouabain. The results of the non-gastric H,K-ATPase mutant were rather similar to that of Na,K-ATPase with exception of dihydro-ouabain that showed a much lower affinity with the non-gastric H,K-ATPase mutant. Docking studies showed that all analogues bind to the same pocket in Na,K-ATPase. However, the amino acids to which hydrogen bonds were formed differed and depended on the availability of hydroxyl or keto groups in the ouabain analogues. Non-gastric H,K-ATPase (dpeaa)DE-He213 Na,K-ATPase (dpeaa)DE-He213 Ouabain (dpeaa)DE-He213 Strophanthidin (dpeaa)DE-He213 Digoxin (dpeaa)DE-He213 Swarts, Herman G. P. verfasserin aut Karawajczyk, Anna verfasserin aut Schaftenaar, Gijs verfasserin aut Willems, Peter H. G. M. verfasserin aut Koenderink, Jan B. verfasserin aut Enthalten in Pflügers Archiv Berlin : Springer, 1868 457(2008), 3 vom: 07. März, Seite 623-634 (DE-627)25463897X (DE-600)1463014-X 1432-2013 nnns volume:457 year:2008 number:3 day:07 month:03 pages:623-634 https://dx.doi.org/10.1007/s00424-008-0467-8 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 42.63 ASE 44.37 ASE AR 457 2008 3 07 03 623-634
spelling	10.1007/s00424-008-0467-8 doi (DE-627)SPR005611555 (SPR)s00424-008-0467-8-e DE-627 ger DE-627 rakwb eng 610 ASE 610 590 ASE 42.63 bkl 44.37 bkl De Pont, Jan Joep H. H. M. verfasserin aut The non-gastric H,K-ATPase as a tool to study the ouabain-binding site in Na,K-ATPase 2008 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Based on studies with chimeras between (non-)gastric H,K-ATPase and Na,K-ATPase, a model for the ouabain binding site has recently been presented (Qiu et al. J.Biol.Chem. 280 (2005) 32349). In this model, hydrogen bonds between specific amino acid residues of Na,K-ATPase and hydroxyl groups of ouabain play a crucial role. In the present study, a series of ouabain analogues were tested on baculovirus-expressed Na,K-ATPase and an ouabain-sensitive mutant of non-gastric H,K-ATPase (D312E/ S319G/ A778P/ I795L/ F802C). For each analogue, the results obtained by measuring ATPase inhibition and [3H]ouabain replacement agreed rather well. In Na,K-ATPase, strophanthidin had a 7–10 times higher and digoxin a 4–12 times lower affinity than ouabain. The results of the non-gastric H,K-ATPase mutant were rather similar to that of Na,K-ATPase with exception of dihydro-ouabain that showed a much lower affinity with the non-gastric H,K-ATPase mutant. Docking studies showed that all analogues bind to the same pocket in Na,K-ATPase. However, the amino acids to which hydrogen bonds were formed differed and depended on the availability of hydroxyl or keto groups in the ouabain analogues. Non-gastric H,K-ATPase (dpeaa)DE-He213 Na,K-ATPase (dpeaa)DE-He213 Ouabain (dpeaa)DE-He213 Strophanthidin (dpeaa)DE-He213 Digoxin (dpeaa)DE-He213 Swarts, Herman G. P. verfasserin aut Karawajczyk, Anna verfasserin aut Schaftenaar, Gijs verfasserin aut Willems, Peter H. G. M. verfasserin aut Koenderink, Jan B. verfasserin aut Enthalten in Pflügers Archiv Berlin : Springer, 1868 457(2008), 3 vom: 07. März, Seite 623-634 (DE-627)25463897X (DE-600)1463014-X 1432-2013 nnns volume:457 year:2008 number:3 day:07 month:03 pages:623-634 https://dx.doi.org/10.1007/s00424-008-0467-8 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 42.63 ASE 44.37 ASE AR 457 2008 3 07 03 623-634
allfields_unstemmed	10.1007/s00424-008-0467-8 doi (DE-627)SPR005611555 (SPR)s00424-008-0467-8-e DE-627 ger DE-627 rakwb eng 610 ASE 610 590 ASE 42.63 bkl 44.37 bkl De Pont, Jan Joep H. H. M. verfasserin aut The non-gastric H,K-ATPase as a tool to study the ouabain-binding site in Na,K-ATPase 2008 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Based on studies with chimeras between (non-)gastric H,K-ATPase and Na,K-ATPase, a model for the ouabain binding site has recently been presented (Qiu et al. J.Biol.Chem. 280 (2005) 32349). In this model, hydrogen bonds between specific amino acid residues of Na,K-ATPase and hydroxyl groups of ouabain play a crucial role. In the present study, a series of ouabain analogues were tested on baculovirus-expressed Na,K-ATPase and an ouabain-sensitive mutant of non-gastric H,K-ATPase (D312E/ S319G/ A778P/ I795L/ F802C). For each analogue, the results obtained by measuring ATPase inhibition and [3H]ouabain replacement agreed rather well. In Na,K-ATPase, strophanthidin had a 7–10 times higher and digoxin a 4–12 times lower affinity than ouabain. The results of the non-gastric H,K-ATPase mutant were rather similar to that of Na,K-ATPase with exception of dihydro-ouabain that showed a much lower affinity with the non-gastric H,K-ATPase mutant. Docking studies showed that all analogues bind to the same pocket in Na,K-ATPase. However, the amino acids to which hydrogen bonds were formed differed and depended on the availability of hydroxyl or keto groups in the ouabain analogues. Non-gastric H,K-ATPase (dpeaa)DE-He213 Na,K-ATPase (dpeaa)DE-He213 Ouabain (dpeaa)DE-He213 Strophanthidin (dpeaa)DE-He213 Digoxin (dpeaa)DE-He213 Swarts, Herman G. P. verfasserin aut Karawajczyk, Anna verfasserin aut Schaftenaar, Gijs verfasserin aut Willems, Peter H. G. M. verfasserin aut Koenderink, Jan B. verfasserin aut Enthalten in Pflügers Archiv Berlin : Springer, 1868 457(2008), 3 vom: 07. März, Seite 623-634 (DE-627)25463897X (DE-600)1463014-X 1432-2013 nnns volume:457 year:2008 number:3 day:07 month:03 pages:623-634 https://dx.doi.org/10.1007/s00424-008-0467-8 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 42.63 ASE 44.37 ASE AR 457 2008 3 07 03 623-634
allfieldsGer	10.1007/s00424-008-0467-8 doi (DE-627)SPR005611555 (SPR)s00424-008-0467-8-e DE-627 ger DE-627 rakwb eng 610 ASE 610 590 ASE 42.63 bkl 44.37 bkl De Pont, Jan Joep H. H. M. verfasserin aut The non-gastric H,K-ATPase as a tool to study the ouabain-binding site in Na,K-ATPase 2008 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Based on studies with chimeras between (non-)gastric H,K-ATPase and Na,K-ATPase, a model for the ouabain binding site has recently been presented (Qiu et al. J.Biol.Chem. 280 (2005) 32349). In this model, hydrogen bonds between specific amino acid residues of Na,K-ATPase and hydroxyl groups of ouabain play a crucial role. In the present study, a series of ouabain analogues were tested on baculovirus-expressed Na,K-ATPase and an ouabain-sensitive mutant of non-gastric H,K-ATPase (D312E/ S319G/ A778P/ I795L/ F802C). For each analogue, the results obtained by measuring ATPase inhibition and [3H]ouabain replacement agreed rather well. In Na,K-ATPase, strophanthidin had a 7–10 times higher and digoxin a 4–12 times lower affinity than ouabain. The results of the non-gastric H,K-ATPase mutant were rather similar to that of Na,K-ATPase with exception of dihydro-ouabain that showed a much lower affinity with the non-gastric H,K-ATPase mutant. Docking studies showed that all analogues bind to the same pocket in Na,K-ATPase. However, the amino acids to which hydrogen bonds were formed differed and depended on the availability of hydroxyl or keto groups in the ouabain analogues. Non-gastric H,K-ATPase (dpeaa)DE-He213 Na,K-ATPase (dpeaa)DE-He213 Ouabain (dpeaa)DE-He213 Strophanthidin (dpeaa)DE-He213 Digoxin (dpeaa)DE-He213 Swarts, Herman G. P. verfasserin aut Karawajczyk, Anna verfasserin aut Schaftenaar, Gijs verfasserin aut Willems, Peter H. G. M. verfasserin aut Koenderink, Jan B. verfasserin aut Enthalten in Pflügers Archiv Berlin : Springer, 1868 457(2008), 3 vom: 07. März, Seite 623-634 (DE-627)25463897X (DE-600)1463014-X 1432-2013 nnns volume:457 year:2008 number:3 day:07 month:03 pages:623-634 https://dx.doi.org/10.1007/s00424-008-0467-8 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 42.63 ASE 44.37 ASE AR 457 2008 3 07 03 623-634
allfieldsSound	10.1007/s00424-008-0467-8 doi (DE-627)SPR005611555 (SPR)s00424-008-0467-8-e DE-627 ger DE-627 rakwb eng 610 ASE 610 590 ASE 42.63 bkl 44.37 bkl De Pont, Jan Joep H. H. M. verfasserin aut The non-gastric H,K-ATPase as a tool to study the ouabain-binding site in Na,K-ATPase 2008 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Based on studies with chimeras between (non-)gastric H,K-ATPase and Na,K-ATPase, a model for the ouabain binding site has recently been presented (Qiu et al. J.Biol.Chem. 280 (2005) 32349). In this model, hydrogen bonds between specific amino acid residues of Na,K-ATPase and hydroxyl groups of ouabain play a crucial role. In the present study, a series of ouabain analogues were tested on baculovirus-expressed Na,K-ATPase and an ouabain-sensitive mutant of non-gastric H,K-ATPase (D312E/ S319G/ A778P/ I795L/ F802C). For each analogue, the results obtained by measuring ATPase inhibition and [3H]ouabain replacement agreed rather well. In Na,K-ATPase, strophanthidin had a 7–10 times higher and digoxin a 4–12 times lower affinity than ouabain. The results of the non-gastric H,K-ATPase mutant were rather similar to that of Na,K-ATPase with exception of dihydro-ouabain that showed a much lower affinity with the non-gastric H,K-ATPase mutant. Docking studies showed that all analogues bind to the same pocket in Na,K-ATPase. However, the amino acids to which hydrogen bonds were formed differed and depended on the availability of hydroxyl or keto groups in the ouabain analogues. Non-gastric H,K-ATPase (dpeaa)DE-He213 Na,K-ATPase (dpeaa)DE-He213 Ouabain (dpeaa)DE-He213 Strophanthidin (dpeaa)DE-He213 Digoxin (dpeaa)DE-He213 Swarts, Herman G. P. verfasserin aut Karawajczyk, Anna verfasserin aut Schaftenaar, Gijs verfasserin aut Willems, Peter H. G. M. verfasserin aut Koenderink, Jan B. verfasserin aut Enthalten in Pflügers Archiv Berlin : Springer, 1868 457(2008), 3 vom: 07. März, Seite 623-634 (DE-627)25463897X (DE-600)1463014-X 1432-2013 nnns volume:457 year:2008 number:3 day:07 month:03 pages:623-634 https://dx.doi.org/10.1007/s00424-008-0467-8 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 42.63 ASE 44.37 ASE AR 457 2008 3 07 03 623-634
language	English
source	Enthalten in Pflügers Archiv 457(2008), 3 vom: 07. März, Seite 623-634 volume:457 year:2008 number:3 day:07 month:03 pages:623-634
sourceStr	Enthalten in Pflügers Archiv 457(2008), 3 vom: 07. März, Seite 623-634 volume:457 year:2008 number:3 day:07 month:03 pages:623-634
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Non-gastric H,K-ATPase Na,K-ATPase Ouabain Strophanthidin Digoxin
dewey-raw	610
isfreeaccess_bool	true
container_title	Pflügers Archiv
authorswithroles_txt_mv	De Pont, Jan Joep H. H. M. @@aut@@ Swarts, Herman G. P. @@aut@@ Karawajczyk, Anna @@aut@@ Schaftenaar, Gijs @@aut@@ Willems, Peter H. G. M. @@aut@@ Koenderink, Jan B. @@aut@@
publishDateDaySort_date	2008-03-07T00:00:00Z
hierarchy_top_id	25463897X
dewey-sort	3610
id	SPR005611555
language_de	englisch
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author	De Pont, Jan Joep H. H. M.
spellingShingle	De Pont, Jan Joep H. H. M. ddc 610 bkl 42.63 bkl 44.37 misc Non-gastric H,K-ATPase misc Na,K-ATPase misc Ouabain misc Strophanthidin misc Digoxin The non-gastric H,K-ATPase as a tool to study the ouabain-binding site in Na,K-ATPase
authorStr	De Pont, Jan Joep H. H. M.
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topic_title	610 ASE 610 590 ASE 42.63 bkl 44.37 bkl The non-gastric H,K-ATPase as a tool to study the ouabain-binding site in Na,K-ATPase Non-gastric H,K-ATPase (dpeaa)DE-He213 Na,K-ATPase (dpeaa)DE-He213 Ouabain (dpeaa)DE-He213 Strophanthidin (dpeaa)DE-He213 Digoxin (dpeaa)DE-He213
topic	ddc 610 bkl 42.63 bkl 44.37 misc Non-gastric H,K-ATPase misc Na,K-ATPase misc Ouabain misc Strophanthidin misc Digoxin
topic_unstemmed	ddc 610 bkl 42.63 bkl 44.37 misc Non-gastric H,K-ATPase misc Na,K-ATPase misc Ouabain misc Strophanthidin misc Digoxin
topic_browse	ddc 610 bkl 42.63 bkl 44.37 misc Non-gastric H,K-ATPase misc Na,K-ATPase misc Ouabain misc Strophanthidin misc Digoxin
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title	The non-gastric H,K-ATPase as a tool to study the ouabain-binding site in Na,K-ATPase
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title_full	The non-gastric H,K-ATPase as a tool to study the ouabain-binding site in Na,K-ATPase
author_sort	De Pont, Jan Joep H. H. M.
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author_browse	De Pont, Jan Joep H. H. M. Swarts, Herman G. P. Karawajczyk, Anna Schaftenaar, Gijs Willems, Peter H. G. M. Koenderink, Jan B.
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class	610 ASE 610 590 ASE 42.63 bkl 44.37 bkl
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author-letter	De Pont, Jan Joep H. H. M.
doi_str_mv	10.1007/s00424-008-0467-8
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title_sort	non-gastric h,k-atpase as a tool to study the ouabain-binding site in na,k-atpase
title_auth	The non-gastric H,K-ATPase as a tool to study the ouabain-binding site in Na,K-ATPase
abstract	Abstract Based on studies with chimeras between (non-)gastric H,K-ATPase and Na,K-ATPase, a model for the ouabain binding site has recently been presented (Qiu et al. J.Biol.Chem. 280 (2005) 32349). In this model, hydrogen bonds between specific amino acid residues of Na,K-ATPase and hydroxyl groups of ouabain play a crucial role. In the present study, a series of ouabain analogues were tested on baculovirus-expressed Na,K-ATPase and an ouabain-sensitive mutant of non-gastric H,K-ATPase (D312E/ S319G/ A778P/ I795L/ F802C). For each analogue, the results obtained by measuring ATPase inhibition and [3H]ouabain replacement agreed rather well. In Na,K-ATPase, strophanthidin had a 7–10 times higher and digoxin a 4–12 times lower affinity than ouabain. The results of the non-gastric H,K-ATPase mutant were rather similar to that of Na,K-ATPase with exception of dihydro-ouabain that showed a much lower affinity with the non-gastric H,K-ATPase mutant. Docking studies showed that all analogues bind to the same pocket in Na,K-ATPase. However, the amino acids to which hydrogen bonds were formed differed and depended on the availability of hydroxyl or keto groups in the ouabain analogues.
abstractGer	Abstract Based on studies with chimeras between (non-)gastric H,K-ATPase and Na,K-ATPase, a model for the ouabain binding site has recently been presented (Qiu et al. J.Biol.Chem. 280 (2005) 32349). In this model, hydrogen bonds between specific amino acid residues of Na,K-ATPase and hydroxyl groups of ouabain play a crucial role. In the present study, a series of ouabain analogues were tested on baculovirus-expressed Na,K-ATPase and an ouabain-sensitive mutant of non-gastric H,K-ATPase (D312E/ S319G/ A778P/ I795L/ F802C). For each analogue, the results obtained by measuring ATPase inhibition and [3H]ouabain replacement agreed rather well. In Na,K-ATPase, strophanthidin had a 7–10 times higher and digoxin a 4–12 times lower affinity than ouabain. The results of the non-gastric H,K-ATPase mutant were rather similar to that of Na,K-ATPase with exception of dihydro-ouabain that showed a much lower affinity with the non-gastric H,K-ATPase mutant. Docking studies showed that all analogues bind to the same pocket in Na,K-ATPase. However, the amino acids to which hydrogen bonds were formed differed and depended on the availability of hydroxyl or keto groups in the ouabain analogues.
abstract_unstemmed	Abstract Based on studies with chimeras between (non-)gastric H,K-ATPase and Na,K-ATPase, a model for the ouabain binding site has recently been presented (Qiu et al. J.Biol.Chem. 280 (2005) 32349). In this model, hydrogen bonds between specific amino acid residues of Na,K-ATPase and hydroxyl groups of ouabain play a crucial role. In the present study, a series of ouabain analogues were tested on baculovirus-expressed Na,K-ATPase and an ouabain-sensitive mutant of non-gastric H,K-ATPase (D312E/ S319G/ A778P/ I795L/ F802C). For each analogue, the results obtained by measuring ATPase inhibition and [3H]ouabain replacement agreed rather well. In Na,K-ATPase, strophanthidin had a 7–10 times higher and digoxin a 4–12 times lower affinity than ouabain. The results of the non-gastric H,K-ATPase mutant were rather similar to that of Na,K-ATPase with exception of dihydro-ouabain that showed a much lower affinity with the non-gastric H,K-ATPase mutant. Docking studies showed that all analogues bind to the same pocket in Na,K-ATPase. However, the amino acids to which hydrogen bonds were formed differed and depended on the availability of hydroxyl or keto groups in the ouabain analogues.
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container_issue	3
title_short	The non-gastric H,K-ATPase as a tool to study the ouabain-binding site in Na,K-ATPase
url	https://dx.doi.org/10.1007/s00424-008-0467-8
remote_bool	true
author2	Swarts, Herman G. P. Karawajczyk, Anna Schaftenaar, Gijs Willems, Peter H. G. M. Koenderink, Jan B.
author2Str	Swarts, Herman G. P. Karawajczyk, Anna Schaftenaar, Gijs Willems, Peter H. G. M. Koenderink, Jan B.
ppnlink	25463897X
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doi_str	10.1007/s00424-008-0467-8
up_date	2024-07-03T17:30:39.913Z
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The non-gastric H,K-ATPase as a tool to study the ouabain-binding site in Na,K-ATPase

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