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| {{STRUCTURE_1qb3| PDB=1qb3 | SCENE= }} | | {{STRUCTURE_1qb3| PDB=1qb3 | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF THE CELL CYCLE REGULATORY PROTEIN CKS1'''
| | ===CRYSTAL STRUCTURE OF THE CELL CYCLE REGULATORY PROTEIN CKS1=== |
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| ==Overview==
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| BACKGROUND: The Saccharomyces cerevisiae protein Cks1 (cyclin-dependent kinase subunit 1) is essential for cell-cycle progression. The biological function of Cks1 can be modulated by a switch between two distinct molecular assemblies: the single domain fold, which results from the closing of a beta-hinge motif, and the intersubunit beta-strand interchanged dimer, which arises from the opening of the beta-hinge motif. The crystal structure of a cyclin-dependent kinase (Cdk) in complex with the human Cks homolog CksHs1 single-domain fold revealed the importance of conserved hydrophobic residues and charged residues within the beta-hinge motif. RESULTS: The 3.0 A resolution Cks1 structure reveals the strict structural conservation of the Cks alpha/beta-core fold and the beta-hinge motif. The beta hinge identified in the Cks1 structure includes a novel pivot and exposes a cluster of conserved tyrosine residues that are involved in Cdk binding but are sequestered in the beta-interchanged Cks homolog suc1 dimer structure. This Cks1 structure confirms the conservation of the Cks anion-binding site, which interacts with sidechain residues from the C-terminal alpha helix of another subunit in the crystal. CONCLUSIONS: The Cks1 structure exemplifies the conservation of the beta-interchanged dimer and the anion-binding site in evolutionarily distant yeast and human Cks homologs. Mutational analyses including in vivo rescue of CKS1 disruption support the dual functional roles of the beta-hinge residue Glu94, which participates in Cdk binding, and of the anion-binding pocket that is located 22 A away and on an opposite face to Glu94. The Cks1 structure suggests a biological role for the beta-interchanged dimer and the anion-binding site in targeting Cdks to specific phosphoproteins during cell-cycle progression.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10997903}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10997903 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10997903}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Cell cycle mutagenesis domain swapping]] | | [[Category: Cell cycle mutagenesis domain swapping]] |
| [[Category: Cyclin-dependent kinase]] | | [[Category: Cyclin-dependent kinase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:05:20 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:31:54 2008'' |