1jst
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(New page: 200px<br /> <applet load="1jst" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jst, resolution 2.6Å" /> '''PHOSPHORYLATED CYCLI...)
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Revision as of 15:37, 12 November 2007
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PHOSPHORYLATED CYCLIN-DEPENDENT KINASE-2 BOUND TO CYCLIN A
Overview
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 Structure
1JST is a Protein complex structure of sequences from Homo sapiens with MN and ATP as ligands. Full crystallographic information is available from OCA.
Reference
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
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