From Crystal Structures of RgIA4 in Complex with <i<Ac</i<-AChBP to Molecular Determinants of Its High Potency of α9α10 nAChR

α9-containing nicotinic acetylcholine receptors (nAChRs) have been shown to play critical roles in neuropathic pain. The α-conotoxin (α-CTx) RgIA and its analog RgIA4 were identified as the most selective inhibitor of α9α10 nAChR. However, the mechanism of their selectivity toward α9α10 nAChR remain...
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Autor*in:	Si Pan [verfasserIn] Yingxu Fan [verfasserIn] Xiaopeng Zhu [verfasserIn] Yi Xue [verfasserIn] Sulan Luo [verfasserIn] Xinquan Wang [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2021

Schlagwörter:	acetylcholine binding protein nicotinic acetylcholine receptors α-conotoxin RgIA RgIA4 crystal structure

Übergeordnetes Werk:	In: Marine Drugs - MDPI AG, 2005, 19(2021), 12, p 709
Übergeordnetes Werk:	volume:19 ; year:2021 ; number:12, p 709

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/md19120709

Katalog-ID:	DOAJ030632110

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allfields	10.3390/md19120709 doi (DE-627)DOAJ030632110 (DE-599)DOAJa922cb020b5e4774b2e4dd886500386d DE-627 ger DE-627 rakwb eng QH301-705.5 Si Pan verfasserin aut From Crystal Structures of RgIA4 in Complex with <i<Ac</i<-AChBP to Molecular Determinants of Its High Potency of α9α10 nAChR 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier α9-containing nicotinic acetylcholine receptors (nAChRs) have been shown to play critical roles in neuropathic pain. The α-conotoxin (α-CTx) RgIA and its analog RgIA4 were identified as the most selective inhibitor of α9α10 nAChR. However, the mechanism of their selectivity toward α9α10 nAChR remains elusive. Here, we reported the co-crystal structure of RgIA and RgIA4 in complex with <i<Aplysia californica</i< acetylcholine binding protein (<i<Ac</i<-AChBP) at resolution of 2.6 Å, respectively. Based on the structure of the complexes, together with molecular dynamic simulation (MD-simulation), we suggested the key residues of α9α10 nAChR in determining its high affinity for RgIA/RgIA4. This is the first time the complex between pain-related conotoxins and <i<Ac</i<-AChBP was reported and the complementary side of α9 subunit in binding of the antagonists shown. These results provide realistic template for the design of new therapeutic in neuropathic pain. acetylcholine binding protein nicotinic acetylcholine receptors α-conotoxin RgIA RgIA4 crystal structure Biology (General) Yingxu Fan verfasserin aut Xiaopeng Zhu verfasserin aut Yi Xue verfasserin aut Sulan Luo verfasserin aut Xinquan Wang verfasserin aut In Marine Drugs MDPI AG, 2005 19(2021), 12, p 709 (DE-627)477992420 (DE-600)2175190-0 16603397 nnns volume:19 year:2021 number:12, p 709 https://doi.org/10.3390/md19120709 kostenfrei https://doaj.org/article/a922cb020b5e4774b2e4dd886500386d kostenfrei https://www.mdpi.com/1660-3397/19/12/709 kostenfrei https://doaj.org/toc/1660-3397 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_381 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 19 2021 12, p 709
spelling	10.3390/md19120709 doi (DE-627)DOAJ030632110 (DE-599)DOAJa922cb020b5e4774b2e4dd886500386d DE-627 ger DE-627 rakwb eng QH301-705.5 Si Pan verfasserin aut From Crystal Structures of RgIA4 in Complex with <i<Ac</i<-AChBP to Molecular Determinants of Its High Potency of α9α10 nAChR 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier α9-containing nicotinic acetylcholine receptors (nAChRs) have been shown to play critical roles in neuropathic pain. The α-conotoxin (α-CTx) RgIA and its analog RgIA4 were identified as the most selective inhibitor of α9α10 nAChR. However, the mechanism of their selectivity toward α9α10 nAChR remains elusive. Here, we reported the co-crystal structure of RgIA and RgIA4 in complex with <i<Aplysia californica</i< acetylcholine binding protein (<i<Ac</i<-AChBP) at resolution of 2.6 Å, respectively. Based on the structure of the complexes, together with molecular dynamic simulation (MD-simulation), we suggested the key residues of α9α10 nAChR in determining its high affinity for RgIA/RgIA4. This is the first time the complex between pain-related conotoxins and <i<Ac</i<-AChBP was reported and the complementary side of α9 subunit in binding of the antagonists shown. These results provide realistic template for the design of new therapeutic in neuropathic pain. acetylcholine binding protein nicotinic acetylcholine receptors α-conotoxin RgIA RgIA4 crystal structure Biology (General) Yingxu Fan verfasserin aut Xiaopeng Zhu verfasserin aut Yi Xue verfasserin aut Sulan Luo verfasserin aut Xinquan Wang verfasserin aut In Marine Drugs MDPI AG, 2005 19(2021), 12, p 709 (DE-627)477992420 (DE-600)2175190-0 16603397 nnns volume:19 year:2021 number:12, p 709 https://doi.org/10.3390/md19120709 kostenfrei https://doaj.org/article/a922cb020b5e4774b2e4dd886500386d kostenfrei https://www.mdpi.com/1660-3397/19/12/709 kostenfrei https://doaj.org/toc/1660-3397 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_381 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 19 2021 12, p 709
allfields_unstemmed	10.3390/md19120709 doi (DE-627)DOAJ030632110 (DE-599)DOAJa922cb020b5e4774b2e4dd886500386d DE-627 ger DE-627 rakwb eng QH301-705.5 Si Pan verfasserin aut From Crystal Structures of RgIA4 in Complex with <i<Ac</i<-AChBP to Molecular Determinants of Its High Potency of α9α10 nAChR 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier α9-containing nicotinic acetylcholine receptors (nAChRs) have been shown to play critical roles in neuropathic pain. The α-conotoxin (α-CTx) RgIA and its analog RgIA4 were identified as the most selective inhibitor of α9α10 nAChR. However, the mechanism of their selectivity toward α9α10 nAChR remains elusive. Here, we reported the co-crystal structure of RgIA and RgIA4 in complex with <i<Aplysia californica</i< acetylcholine binding protein (<i<Ac</i<-AChBP) at resolution of 2.6 Å, respectively. Based on the structure of the complexes, together with molecular dynamic simulation (MD-simulation), we suggested the key residues of α9α10 nAChR in determining its high affinity for RgIA/RgIA4. This is the first time the complex between pain-related conotoxins and <i<Ac</i<-AChBP was reported and the complementary side of α9 subunit in binding of the antagonists shown. These results provide realistic template for the design of new therapeutic in neuropathic pain. acetylcholine binding protein nicotinic acetylcholine receptors α-conotoxin RgIA RgIA4 crystal structure Biology (General) Yingxu Fan verfasserin aut Xiaopeng Zhu verfasserin aut Yi Xue verfasserin aut Sulan Luo verfasserin aut Xinquan Wang verfasserin aut In Marine Drugs MDPI AG, 2005 19(2021), 12, p 709 (DE-627)477992420 (DE-600)2175190-0 16603397 nnns volume:19 year:2021 number:12, p 709 https://doi.org/10.3390/md19120709 kostenfrei https://doaj.org/article/a922cb020b5e4774b2e4dd886500386d kostenfrei https://www.mdpi.com/1660-3397/19/12/709 kostenfrei https://doaj.org/toc/1660-3397 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_381 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 19 2021 12, p 709
allfieldsGer	10.3390/md19120709 doi (DE-627)DOAJ030632110 (DE-599)DOAJa922cb020b5e4774b2e4dd886500386d DE-627 ger DE-627 rakwb eng QH301-705.5 Si Pan verfasserin aut From Crystal Structures of RgIA4 in Complex with <i<Ac</i<-AChBP to Molecular Determinants of Its High Potency of α9α10 nAChR 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier α9-containing nicotinic acetylcholine receptors (nAChRs) have been shown to play critical roles in neuropathic pain. The α-conotoxin (α-CTx) RgIA and its analog RgIA4 were identified as the most selective inhibitor of α9α10 nAChR. However, the mechanism of their selectivity toward α9α10 nAChR remains elusive. Here, we reported the co-crystal structure of RgIA and RgIA4 in complex with <i<Aplysia californica</i< acetylcholine binding protein (<i<Ac</i<-AChBP) at resolution of 2.6 Å, respectively. Based on the structure of the complexes, together with molecular dynamic simulation (MD-simulation), we suggested the key residues of α9α10 nAChR in determining its high affinity for RgIA/RgIA4. This is the first time the complex between pain-related conotoxins and <i<Ac</i<-AChBP was reported and the complementary side of α9 subunit in binding of the antagonists shown. These results provide realistic template for the design of new therapeutic in neuropathic pain. acetylcholine binding protein nicotinic acetylcholine receptors α-conotoxin RgIA RgIA4 crystal structure Biology (General) Yingxu Fan verfasserin aut Xiaopeng Zhu verfasserin aut Yi Xue verfasserin aut Sulan Luo verfasserin aut Xinquan Wang verfasserin aut In Marine Drugs MDPI AG, 2005 19(2021), 12, p 709 (DE-627)477992420 (DE-600)2175190-0 16603397 nnns volume:19 year:2021 number:12, p 709 https://doi.org/10.3390/md19120709 kostenfrei https://doaj.org/article/a922cb020b5e4774b2e4dd886500386d kostenfrei https://www.mdpi.com/1660-3397/19/12/709 kostenfrei https://doaj.org/toc/1660-3397 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_381 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 19 2021 12, p 709
allfieldsSound	10.3390/md19120709 doi (DE-627)DOAJ030632110 (DE-599)DOAJa922cb020b5e4774b2e4dd886500386d DE-627 ger DE-627 rakwb eng QH301-705.5 Si Pan verfasserin aut From Crystal Structures of RgIA4 in Complex with <i<Ac</i<-AChBP to Molecular Determinants of Its High Potency of α9α10 nAChR 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier α9-containing nicotinic acetylcholine receptors (nAChRs) have been shown to play critical roles in neuropathic pain. The α-conotoxin (α-CTx) RgIA and its analog RgIA4 were identified as the most selective inhibitor of α9α10 nAChR. However, the mechanism of their selectivity toward α9α10 nAChR remains elusive. Here, we reported the co-crystal structure of RgIA and RgIA4 in complex with <i<Aplysia californica</i< acetylcholine binding protein (<i<Ac</i<-AChBP) at resolution of 2.6 Å, respectively. Based on the structure of the complexes, together with molecular dynamic simulation (MD-simulation), we suggested the key residues of α9α10 nAChR in determining its high affinity for RgIA/RgIA4. This is the first time the complex between pain-related conotoxins and <i<Ac</i<-AChBP was reported and the complementary side of α9 subunit in binding of the antagonists shown. These results provide realistic template for the design of new therapeutic in neuropathic pain. acetylcholine binding protein nicotinic acetylcholine receptors α-conotoxin RgIA RgIA4 crystal structure Biology (General) Yingxu Fan verfasserin aut Xiaopeng Zhu verfasserin aut Yi Xue verfasserin aut Sulan Luo verfasserin aut Xinquan Wang verfasserin aut In Marine Drugs MDPI AG, 2005 19(2021), 12, p 709 (DE-627)477992420 (DE-600)2175190-0 16603397 nnns volume:19 year:2021 number:12, p 709 https://doi.org/10.3390/md19120709 kostenfrei https://doaj.org/article/a922cb020b5e4774b2e4dd886500386d kostenfrei https://www.mdpi.com/1660-3397/19/12/709 kostenfrei https://doaj.org/toc/1660-3397 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_381 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 19 2021 12, p 709
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topic_facet	acetylcholine binding protein nicotinic acetylcholine receptors α-conotoxin RgIA RgIA4 crystal structure Biology (General)
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container_title	Marine Drugs
authorswithroles_txt_mv	Si Pan @@aut@@ Yingxu Fan @@aut@@ Xiaopeng Zhu @@aut@@ Yi Xue @@aut@@ Sulan Luo @@aut@@ Xinquan Wang @@aut@@
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callnumber-first	Q - Science
author	Si Pan
spellingShingle	Si Pan misc QH301-705.5 misc acetylcholine binding protein misc nicotinic acetylcholine receptors misc α-conotoxin misc RgIA misc RgIA4 misc crystal structure misc Biology (General) From Crystal Structures of RgIA4 in Complex with <i<Ac</i<-AChBP to Molecular Determinants of Its High Potency of α9α10 nAChR
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topic_title	QH301-705.5 From Crystal Structures of RgIA4 in Complex with <i<Ac</i<-AChBP to Molecular Determinants of Its High Potency of α9α10 nAChR acetylcholine binding protein nicotinic acetylcholine receptors α-conotoxin RgIA RgIA4 crystal structure
topic	misc QH301-705.5 misc acetylcholine binding protein misc nicotinic acetylcholine receptors misc α-conotoxin misc RgIA misc RgIA4 misc crystal structure misc Biology (General)
topic_unstemmed	misc QH301-705.5 misc acetylcholine binding protein misc nicotinic acetylcholine receptors misc α-conotoxin misc RgIA misc RgIA4 misc crystal structure misc Biology (General)
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title	From Crystal Structures of RgIA4 in Complex with <i<Ac</i<-AChBP to Molecular Determinants of Its High Potency of α9α10 nAChR
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title_full	From Crystal Structures of RgIA4 in Complex with <i<Ac</i<-AChBP to Molecular Determinants of Its High Potency of α9α10 nAChR
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title_sort	from crystal structures of rgia4 in complex with <i<ac</i<-achbp to molecular determinants of its high potency of α9α10 nachr
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title_auth	From Crystal Structures of RgIA4 in Complex with <i<Ac</i<-AChBP to Molecular Determinants of Its High Potency of α9α10 nAChR
abstract	α9-containing nicotinic acetylcholine receptors (nAChRs) have been shown to play critical roles in neuropathic pain. The α-conotoxin (α-CTx) RgIA and its analog RgIA4 were identified as the most selective inhibitor of α9α10 nAChR. However, the mechanism of their selectivity toward α9α10 nAChR remains elusive. Here, we reported the co-crystal structure of RgIA and RgIA4 in complex with <i<Aplysia californica</i< acetylcholine binding protein (<i<Ac</i<-AChBP) at resolution of 2.6 Å, respectively. Based on the structure of the complexes, together with molecular dynamic simulation (MD-simulation), we suggested the key residues of α9α10 nAChR in determining its high affinity for RgIA/RgIA4. This is the first time the complex between pain-related conotoxins and <i<Ac</i<-AChBP was reported and the complementary side of α9 subunit in binding of the antagonists shown. These results provide realistic template for the design of new therapeutic in neuropathic pain.
abstractGer	α9-containing nicotinic acetylcholine receptors (nAChRs) have been shown to play critical roles in neuropathic pain. The α-conotoxin (α-CTx) RgIA and its analog RgIA4 were identified as the most selective inhibitor of α9α10 nAChR. However, the mechanism of their selectivity toward α9α10 nAChR remains elusive. Here, we reported the co-crystal structure of RgIA and RgIA4 in complex with <i<Aplysia californica</i< acetylcholine binding protein (<i<Ac</i<-AChBP) at resolution of 2.6 Å, respectively. Based on the structure of the complexes, together with molecular dynamic simulation (MD-simulation), we suggested the key residues of α9α10 nAChR in determining its high affinity for RgIA/RgIA4. This is the first time the complex between pain-related conotoxins and <i<Ac</i<-AChBP was reported and the complementary side of α9 subunit in binding of the antagonists shown. These results provide realistic template for the design of new therapeutic in neuropathic pain.
abstract_unstemmed	α9-containing nicotinic acetylcholine receptors (nAChRs) have been shown to play critical roles in neuropathic pain. The α-conotoxin (α-CTx) RgIA and its analog RgIA4 were identified as the most selective inhibitor of α9α10 nAChR. However, the mechanism of their selectivity toward α9α10 nAChR remains elusive. Here, we reported the co-crystal structure of RgIA and RgIA4 in complex with <i<Aplysia californica</i< acetylcholine binding protein (<i<Ac</i<-AChBP) at resolution of 2.6 Å, respectively. Based on the structure of the complexes, together with molecular dynamic simulation (MD-simulation), we suggested the key residues of α9α10 nAChR in determining its high affinity for RgIA/RgIA4. This is the first time the complex between pain-related conotoxins and <i<Ac</i<-AChBP was reported and the complementary side of α9 subunit in binding of the antagonists shown. These results provide realistic template for the design of new therapeutic in neuropathic pain.
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title_short	From Crystal Structures of RgIA4 in Complex with <i<Ac</i<-AChBP to Molecular Determinants of Its High Potency of α9α10 nAChR
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From Crystal Structures of RgIA4 in Complex with <i<Ac</i<-AChBP to Molecular Determinants of Its High Potency of α9α10 nAChR

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