Substrate-Specificity of Cdc2 Kinase from Human HeLa-Cells as Determined with Synthetic Peptides and Molecular Modeling
A systematic study was undertaken in order to assess the substrate specificity of cyclin-B/cell division control protein kinase (CDC2) isolated from human HeLa cells, using 13-15 residue peptides with a central histone-like KKSPKK motif as a model. Replacement of the proline residue by any of the ot...
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E-Artikel |
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Englisch |
| Erschienen: |
1994 |
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Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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in: Archives of Biochemistry and Biophysics - Amsterdam : Elsevier, 315(1994), 2, Seite 415-424 |
| Übergeordnetes Werk: |
volume:315 ; year:1994 ; number:2 ; pages:415-424 |
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| 520 | |a A systematic study was undertaken in order to assess the substrate specificity of cyclin-B/cell division control protein kinase (CDC2) isolated from human HeLa cells, using 13-15 residue peptides with a central histone-like KKSPKK motif as a model. Replacement of the proline residue by any of the other 19 amino acids or D-proline drastically reduces or abolishes phosphorylation by CDC2. Changing the basic residues to Ala on either side of the -SP- structure differentially reduces phosphorylation. Molecular modeling and dynamics simulation indicated that the phosphorylation site of the peptide may have to adopt a turn-like conformation that will orientate the charged and hydrophobic residues so as to allow interaction with postulated binding surfaces within the CDCS active site. It thus appears that, of the 20 coded amino acids, only proline can provide this conformation in short peptides. This is in agreement with the finding that sarcosine can replace proline in this respect (S. Ando et al. Biochem. Biophys. Res. Commun. 195, 837-843, 1993). | ||
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(DE-627)NLEJ183344235 (DE-599)GBVNLZ183344235 DE-627 ger DE-627 rakwb eng Substrate-Specificity of Cdc2 Kinase from Human HeLa-Cells as Determined with Synthetic Peptides and Molecular Modeling 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A systematic study was undertaken in order to assess the substrate specificity of cyclin-B/cell division control protein kinase (CDC2) isolated from human HeLa cells, using 13-15 residue peptides with a central histone-like KKSPKK motif as a model. Replacement of the proline residue by any of the other 19 amino acids or D-proline drastically reduces or abolishes phosphorylation by CDC2. Changing the basic residues to Ala on either side of the -SP- structure differentially reduces phosphorylation. Molecular modeling and dynamics simulation indicated that the phosphorylation site of the peptide may have to adopt a turn-like conformation that will orientate the charged and hydrophobic residues so as to allow interaction with postulated binding surfaces within the CDCS active site. It thus appears that, of the 20 coded amino acids, only proline can provide this conformation in short peptides. This is in agreement with the finding that sarcosine can replace proline in this respect (S. Ando et al. Biochem. Biophys. Res. Commun. 195, 837-843, 1993). Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Zhang, J.W. oth Sanchez, R.J. oth Wang, S.L. oth Guarnaccia, C. oth Tossi, A. oth Zahariev, S. oth Pongor, S. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 315(1994), 2, Seite 415-424 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:315 year:1994 number:2 pages:415-424 http://dx.doi.org/10.1006/abbi.1994.1519 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 315 1994 2 415-424 |
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(DE-627)NLEJ183344235 (DE-599)GBVNLZ183344235 DE-627 ger DE-627 rakwb eng Substrate-Specificity of Cdc2 Kinase from Human HeLa-Cells as Determined with Synthetic Peptides and Molecular Modeling 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A systematic study was undertaken in order to assess the substrate specificity of cyclin-B/cell division control protein kinase (CDC2) isolated from human HeLa cells, using 13-15 residue peptides with a central histone-like KKSPKK motif as a model. Replacement of the proline residue by any of the other 19 amino acids or D-proline drastically reduces or abolishes phosphorylation by CDC2. Changing the basic residues to Ala on either side of the -SP- structure differentially reduces phosphorylation. Molecular modeling and dynamics simulation indicated that the phosphorylation site of the peptide may have to adopt a turn-like conformation that will orientate the charged and hydrophobic residues so as to allow interaction with postulated binding surfaces within the CDCS active site. It thus appears that, of the 20 coded amino acids, only proline can provide this conformation in short peptides. This is in agreement with the finding that sarcosine can replace proline in this respect (S. Ando et al. Biochem. Biophys. Res. Commun. 195, 837-843, 1993). Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Zhang, J.W. oth Sanchez, R.J. oth Wang, S.L. oth Guarnaccia, C. oth Tossi, A. oth Zahariev, S. oth Pongor, S. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 315(1994), 2, Seite 415-424 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:315 year:1994 number:2 pages:415-424 http://dx.doi.org/10.1006/abbi.1994.1519 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 315 1994 2 415-424 |
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(DE-627)NLEJ183344235 (DE-599)GBVNLZ183344235 DE-627 ger DE-627 rakwb eng Substrate-Specificity of Cdc2 Kinase from Human HeLa-Cells as Determined with Synthetic Peptides and Molecular Modeling 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A systematic study was undertaken in order to assess the substrate specificity of cyclin-B/cell division control protein kinase (CDC2) isolated from human HeLa cells, using 13-15 residue peptides with a central histone-like KKSPKK motif as a model. Replacement of the proline residue by any of the other 19 amino acids or D-proline drastically reduces or abolishes phosphorylation by CDC2. Changing the basic residues to Ala on either side of the -SP- structure differentially reduces phosphorylation. Molecular modeling and dynamics simulation indicated that the phosphorylation site of the peptide may have to adopt a turn-like conformation that will orientate the charged and hydrophobic residues so as to allow interaction with postulated binding surfaces within the CDCS active site. It thus appears that, of the 20 coded amino acids, only proline can provide this conformation in short peptides. This is in agreement with the finding that sarcosine can replace proline in this respect (S. Ando et al. Biochem. Biophys. Res. Commun. 195, 837-843, 1993). Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Zhang, J.W. oth Sanchez, R.J. oth Wang, S.L. oth Guarnaccia, C. oth Tossi, A. oth Zahariev, S. oth Pongor, S. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 315(1994), 2, Seite 415-424 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:315 year:1994 number:2 pages:415-424 http://dx.doi.org/10.1006/abbi.1994.1519 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 315 1994 2 415-424 |
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(DE-627)NLEJ183344235 (DE-599)GBVNLZ183344235 DE-627 ger DE-627 rakwb eng Substrate-Specificity of Cdc2 Kinase from Human HeLa-Cells as Determined with Synthetic Peptides and Molecular Modeling 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A systematic study was undertaken in order to assess the substrate specificity of cyclin-B/cell division control protein kinase (CDC2) isolated from human HeLa cells, using 13-15 residue peptides with a central histone-like KKSPKK motif as a model. Replacement of the proline residue by any of the other 19 amino acids or D-proline drastically reduces or abolishes phosphorylation by CDC2. Changing the basic residues to Ala on either side of the -SP- structure differentially reduces phosphorylation. Molecular modeling and dynamics simulation indicated that the phosphorylation site of the peptide may have to adopt a turn-like conformation that will orientate the charged and hydrophobic residues so as to allow interaction with postulated binding surfaces within the CDCS active site. It thus appears that, of the 20 coded amino acids, only proline can provide this conformation in short peptides. This is in agreement with the finding that sarcosine can replace proline in this respect (S. Ando et al. Biochem. Biophys. Res. Commun. 195, 837-843, 1993). Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Zhang, J.W. oth Sanchez, R.J. oth Wang, S.L. oth Guarnaccia, C. oth Tossi, A. oth Zahariev, S. oth Pongor, S. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 315(1994), 2, Seite 415-424 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:315 year:1994 number:2 pages:415-424 http://dx.doi.org/10.1006/abbi.1994.1519 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 315 1994 2 415-424 |
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(DE-627)NLEJ183344235 (DE-599)GBVNLZ183344235 DE-627 ger DE-627 rakwb eng Substrate-Specificity of Cdc2 Kinase from Human HeLa-Cells as Determined with Synthetic Peptides and Molecular Modeling 1994 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A systematic study was undertaken in order to assess the substrate specificity of cyclin-B/cell division control protein kinase (CDC2) isolated from human HeLa cells, using 13-15 residue peptides with a central histone-like KKSPKK motif as a model. Replacement of the proline residue by any of the other 19 amino acids or D-proline drastically reduces or abolishes phosphorylation by CDC2. Changing the basic residues to Ala on either side of the -SP- structure differentially reduces phosphorylation. Molecular modeling and dynamics simulation indicated that the phosphorylation site of the peptide may have to adopt a turn-like conformation that will orientate the charged and hydrophobic residues so as to allow interaction with postulated binding surfaces within the CDCS active site. It thus appears that, of the 20 coded amino acids, only proline can provide this conformation in short peptides. This is in agreement with the finding that sarcosine can replace proline in this respect (S. Ando et al. Biochem. Biophys. Res. Commun. 195, 837-843, 1993). Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Zhang, J.W. oth Sanchez, R.J. oth Wang, S.L. oth Guarnaccia, C. oth Tossi, A. oth Zahariev, S. oth Pongor, S. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 315(1994), 2, Seite 415-424 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:315 year:1994 number:2 pages:415-424 http://dx.doi.org/10.1006/abbi.1994.1519 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 315 1994 2 415-424 |
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Substrate-Specificity of Cdc2 Kinase from Human HeLa-Cells as Determined with Synthetic Peptides and Molecular Modeling |
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A systematic study was undertaken in order to assess the substrate specificity of cyclin-B/cell division control protein kinase (CDC2) isolated from human HeLa cells, using 13-15 residue peptides with a central histone-like KKSPKK motif as a model. Replacement of the proline residue by any of the other 19 amino acids or D-proline drastically reduces or abolishes phosphorylation by CDC2. Changing the basic residues to Ala on either side of the -SP- structure differentially reduces phosphorylation. Molecular modeling and dynamics simulation indicated that the phosphorylation site of the peptide may have to adopt a turn-like conformation that will orientate the charged and hydrophobic residues so as to allow interaction with postulated binding surfaces within the CDCS active site. It thus appears that, of the 20 coded amino acids, only proline can provide this conformation in short peptides. This is in agreement with the finding that sarcosine can replace proline in this respect (S. Ando et al. Biochem. Biophys. Res. Commun. 195, 837-843, 1993). |
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A systematic study was undertaken in order to assess the substrate specificity of cyclin-B/cell division control protein kinase (CDC2) isolated from human HeLa cells, using 13-15 residue peptides with a central histone-like KKSPKK motif as a model. Replacement of the proline residue by any of the other 19 amino acids or D-proline drastically reduces or abolishes phosphorylation by CDC2. Changing the basic residues to Ala on either side of the -SP- structure differentially reduces phosphorylation. Molecular modeling and dynamics simulation indicated that the phosphorylation site of the peptide may have to adopt a turn-like conformation that will orientate the charged and hydrophobic residues so as to allow interaction with postulated binding surfaces within the CDCS active site. It thus appears that, of the 20 coded amino acids, only proline can provide this conformation in short peptides. This is in agreement with the finding that sarcosine can replace proline in this respect (S. Ando et al. Biochem. Biophys. Res. Commun. 195, 837-843, 1993). |
| abstract_unstemmed |
A systematic study was undertaken in order to assess the substrate specificity of cyclin-B/cell division control protein kinase (CDC2) isolated from human HeLa cells, using 13-15 residue peptides with a central histone-like KKSPKK motif as a model. Replacement of the proline residue by any of the other 19 amino acids or D-proline drastically reduces or abolishes phosphorylation by CDC2. Changing the basic residues to Ala on either side of the -SP- structure differentially reduces phosphorylation. Molecular modeling and dynamics simulation indicated that the phosphorylation site of the peptide may have to adopt a turn-like conformation that will orientate the charged and hydrophobic residues so as to allow interaction with postulated binding surfaces within the CDCS active site. It thus appears that, of the 20 coded amino acids, only proline can provide this conformation in short peptides. This is in agreement with the finding that sarcosine can replace proline in this respect (S. Ando et al. Biochem. Biophys. Res. Commun. 195, 837-843, 1993). |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ183344235</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706201123.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070505s1994 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ183344235</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ183344235</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Substrate-Specificity of Cdc2 Kinase from Human HeLa-Cells as Determined with Synthetic Peptides and Molecular Modeling</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1994</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">A systematic study was undertaken in order to assess the substrate specificity of cyclin-B/cell division control protein kinase (CDC2) isolated from human HeLa cells, using 13-15 residue peptides with a central histone-like KKSPKK motif as a model. Replacement of the proline residue by any of the other 19 amino acids or D-proline drastically reduces or abolishes phosphorylation by CDC2. Changing the basic residues to Ala on either side of the -SP- structure differentially reduces phosphorylation. Molecular modeling and dynamics simulation indicated that the phosphorylation site of the peptide may have to adopt a turn-like conformation that will orientate the charged and hydrophobic residues so as to allow interaction with postulated binding surfaces within the CDCS active site. It thus appears that, of the 20 coded amino acids, only proline can provide this conformation in short peptides. This is in agreement with the finding that sarcosine can replace proline in this respect (S. Ando et al. Biochem. Biophys. Res. Commun. 195, 837-843, 1993).</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Elsevier Journal Backfiles on ScienceDirect 1907 - 2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Zhang, J.W.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Sanchez, R.J.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wang, S.L.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Guarnaccia, C.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Tossi, A.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Zahariev, S.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Pongor, S.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Archives of Biochemistry and Biophysics</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">315(1994), 2, Seite 415-424</subfield><subfield code="w">(DE-627)NLEJ177020539</subfield><subfield code="w">(DE-600)1461378-5</subfield><subfield code="x">0003-9861</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:315</subfield><subfield code="g">year:1994</subfield><subfield code="g">number:2</subfield><subfield code="g">pages:415-424</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1006/abbi.1994.1519</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_H</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SDJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">315</subfield><subfield code="j">1994</subfield><subfield code="e">2</subfield><subfield code="h">415-424</subfield></datafield></record></collection>
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