1jst: Difference between revisions
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[[Image:1jst.gif|left|200px]] | [[Image:1jst.gif|left|200px]] | ||
'''PHOSPHORYLATED CYCLIN-DEPENDENT KINASE-2 BOUND TO CYCLIN A''' | {{Structure | ||
|PDB= 1jst |SIZE=350|CAPTION= <scene name='initialview01'>1jst</scene>, resolution 2.6Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''PHOSPHORYLATED CYCLIN-DEPENDENT KINASE-2 BOUND TO CYCLIN A''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1JST is a [ | 1JST is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JST OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8756328 8756328] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:07:58 2008'' | ||
Revision as of 13:07, 20 March 2008
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| , resolution 2.6Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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