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Substrate specificity of CDC2 kinase from human HeLa cells as determined with synthetic peptides and molecular modelling

J. ZHANG
•
R. J. SANCHEZ
•
S. LUNG
altro
S. PONGOR
1995
  • journal article

Periodico
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Abstract
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).
DOI
10.1006/abbi.1994.1519
WOS
WOS:A1994PV82900028
Archivio
http://hdl.handle.net/11368/1708358
info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-0028021003
Diritti
metadata only access
Soggetti
  • Cdc2 Kinase

  • model peptide

  • molecular modelling

Scopus© citazioni
20
Data di acquisizione
Jun 14, 2022
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Web of Science© citazioni
21
Data di acquisizione
Mar 27, 2024
Visualizzazioni
4
Data di acquisizione
Apr 19, 2024
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