Linked Life Data

10997903

Source:http://linkedlifedata.com/resource/pubmed/id/10997903

Statements in which the resource exists.
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pubmed-article:10997903pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:10997903pubmed:articleTitleCrystal structure and mutational analysis of the Saccharomyces cerevisiae cell cycle regulatory protein Cks1: implications for domain swapping, anion binding and protein interactions.lld:pubmed
pubmed-article:10997903pubmed:affiliationCentre National de la Recherche Scientifique, Marseille, France. yves@afmb.cnrs-mrs.frlld:pubmed
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