1jst
From Proteopedia
(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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- | [[Image:1jst.gif|left|200px]]<br /> | + | [[Image:1jst.gif|left|200px]]<br /><applet load="1jst" size="350" color="white" frame="true" align="right" spinBox="true" |
- | <applet load="1jst" size=" | + | |
caption="1jst, resolution 2.6Å" /> | caption="1jst, resolution 2.6Å" /> | ||
'''PHOSPHORYLATED CYCLIN-DEPENDENT KINASE-2 BOUND TO CYCLIN A'''<br /> | '''PHOSPHORYLATED CYCLIN-DEPENDENT KINASE-2 BOUND TO CYCLIN A'''<br /> | ||
==Overview== | ==Overview== | ||
- | Cyclin-dependent kinase (CDK)-cyclin complexes require phosphorylation on | + | 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== | ==About this Structure== | ||
- | 1JST is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MN and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1JST is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JST OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
- | [[Category: Jeffrey, P | + | [[Category: Jeffrey, P D.]] |
- | [[Category: Pavletich, N | + | [[Category: Pavletich, N P.]] |
- | [[Category: Russo, A | + | [[Category: Russo, A A.]] |
[[Category: ATP]] | [[Category: ATP]] | ||
[[Category: MN]] | [[Category: MN]] | ||
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[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:26:22 2008'' |
Revision as of 11:26, 21 February 2008
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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 and 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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