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- W2529557673 abstract "Many of the important decisions in the cell division cy- cle are determined by cyclin-dependent kinases (CDKs). Members of this family of- serine/threonine protein ki- nases are broadly similar in sequence and, more signif- icantly, each needs to bind to a member of the cyclin family in order to become active as a kinase. In addi- tion, the association between each cyclin and CDK pair, and the activity of the resulting cyclin-CDK complex, are both closely regulated by phosphorylation of the CDK subunit. Once activated, cyclir<DK complexes are re- sponsible for phosphorylating substrates that are required for cell-cycle transitions, such as entry into mitosis or the initiation of DNA synthesis. Insights into the cyclin-CDK interaction and its regu- lation by phosphorylation have come from genetic and biochemical analyses, but such studies are not able to ex- plain why the CDK subunit is inactive in the monomer form, how the kinase is activated by binding cyclin, or how the phosphorylation of particular residues modi- fies kin?e activity. With the resolution by De Bondt et aE. [l] of the crystal structure of one member of the CDK family, human CDK2, in a complex with ATP, we can go some way towards anmering these fundamental questions. In this review, I shall first briefly outline our present knowledge of the regulation of CDKs by cyclins and by phosphorylation, obtained from biochemical and molecular biological analyses, and then discuss how the crystal structure of CDK2 provides an understanding of these phenomena at the molecular level. of a CDKl threonine residue that is conserved in all species [3] - Tl61 in frogs and mammals, T167 in the fis- sion yeast Schizosaccbarornycespombe - the equivalent in CDK2 of which is" @default.
- W2529557673 created "2016-10-14" @default.
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- W2529557673 date "1993-01-01" @default.
- W2529557673 modified "2023-09-27" @default.
- W2529557673 title "The newly resolved crystal structure of CDK2 gives us a tantalizing glimpse of the mechanisms underlying the regulation of cyclin-dependent kinases by cyclins and by phosphorylation." @default.
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