1jst: Difference between revisions
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'''PHOSPHORYLATED CYCLIN-DEPENDENT KINASE-2 BOUND TO CYCLIN A''' | '''PHOSPHORYLATED CYCLIN-DEPENDENT KINASE-2 BOUND TO CYCLIN A''' | ||
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[[Category: Pavletich, N P.]] | [[Category: Pavletich, N P.]] | ||
[[Category: Russo, A A.]] | [[Category: Russo, A A.]] | ||
[[Category: | [[Category: Cdk]] | ||
[[Category: | [[Category: Cyclin]] | ||
[[Category: | [[Category: Phosphorylation]] | ||
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Revision as of 21:51, 2 May 2008
PHOSPHORYLATED CYCLIN-DEPENDENT KINASE-2 BOUND TO CYCLIN A
OverviewOverview
Cyclin-dependent kinase (CDK)-cyclin complexes require phosphorylation on the CDK subunit for full activation of their Ser/Thr protein kinase activity. The crystal structure of the phosphorylated CDK2-CyclinA-ATP gamma S complex has been determined at 2.6 A resolution. The phosphate group, which is on the regulatory T-loop of CDK2, is mostly buried, its charge being neutralized by three Arg side chains. The arginines help extend the influence of the phosphate group through a network of hydrogen bonds to both CDK2 and cyclinA. Comparison with the unphosphorylated CDK2-CyclinA complex shows that the T-loop moves by as much as 7 A, and this affects the putative substrate binding site as well as resulting in additional CDK2-CyclinA contacts. The phosphate group thus acts as a major organizing centre in the CDK2-CyclinA complex.
About this StructureAbout this Structure
1JST is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of cyclin-dependent kinase activation by phosphorylation., Russo AA, Jeffrey PD, Pavletich NP, Nat Struct Biol. 1996 Aug;3(8):696-700. PMID:8756328 Page seeded by OCA on Fri May 2 21:51:38 2008