1jst
From Proteopedia
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|PDB= 1jst |SIZE=350|CAPTION= <scene name='initialview01'>1jst</scene>, resolution 2.6Å | |PDB= 1jst |SIZE=350|CAPTION= <scene name='initialview01'>1jst</scene>, resolution 2.6Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> | + | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jst OCA], [http://www.ebi.ac.uk/pdbsum/1jst PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jst RCSB]</span> | ||
}} | }} | ||
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[[Category: Pavletich, N P.]] | [[Category: Pavletich, N P.]] | ||
[[Category: Russo, A A.]] | [[Category: Russo, A A.]] | ||
| - | [[Category: ATP]] | ||
| - | [[Category: MN]] | ||
[[Category: cdk]] | [[Category: cdk]] | ||
[[Category: complex (protein kinase/cyclin)]] | [[Category: complex (protein kinase/cyclin)]] | ||
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[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:38:27 2008'' |
Revision as of 18:38, 30 March 2008
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| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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