1buh
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(New page: 200px<br /> <applet load="1buh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1buh, resolution 2.6Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 14:08, 12 November 2007
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CRYSTAL STRUCTURE OF THE HUMAN CDK2 KINASE COMPLEX WITH CELL CYCLE-REGULATORY PROTEIN CKSHS1
Overview
The 2.6 Angstrom crystal structure for human cyclin-dependent kinase, 2(CDK2) in complex with CksHs1, a human homolog of essential yeast cell, cycle-regulatory proteins suc1 and Cks1, reveals that CksHs1 binds via all, four beta strands to the kinase C-terminal lobe. This interface is, biologically critical, based upon mutational analysis, but far from the, CDK2 N-terminal lobe, cyclin, and regulatory phosphorylation sites. CDK2, binds the Cks single domain conformation and interacts with conserved, hydrophobic residues plus His-60 and Glu-63 in their closed beta-hinge, motif conformation. The beta hinge opening to form the Cks, beta-interchanged dimer sterically precludes CDK2 binding, providing a, possible mechanism regulating CDK2-Cks interactions. One face of the, complex exposes the sequence-conserved phosphate-binding region on Cks and, the ATP-binding site on CDK2, suggesting that CKs may target CDK2 to other, phosphoproteins during the cell cycle.
About this Structure
1BUH is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1., Bourne Y, Watson MH, Hickey MJ, Holmes W, Rocque W, Reed SI, Tainer JA, Cell. 1996 Mar 22;84(6):863-74. PMID:8601310
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