1FIN
CYCLIN A-CYCLIN-DEPENDENT KINASE 2 COMPLEX
Summary for 1FIN
Entry DOI | 10.2210/pdb1fin/pdb |
Descriptor | CYCLIN-DEPENDENT KINASE 2, CYCLIN A, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total) |
Functional Keywords | complex (transferase-cyclin), cyclin, cdk, phosphorylation, complex (transferase-cyclin) complex, complex (transferase/cyclin) |
Biological source | Homo sapiens (human) More |
Cellular location | Nucleus: P20248 |
Total number of polymer chains | 4 |
Total formula weight | 128702.36 |
Authors | Jeffrey, P.D.,Russo, A.A.,Pavletich, N.P. (deposition date: 1996-07-14, release date: 1997-01-27, Last modification date: 2024-02-07) |
Primary citation | Jeffrey, P.D.,Russo, A.A.,Polyak, K.,Gibbs, E.,Hurwitz, J.,Massague, J.,Pavletich, N.P. Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Nature, 376:313-320, 1995 Cited by PubMed Abstract: The crystal structure of the human cyclinA-cyclin-dependent kinase2 (CDK2)-ATP complex has been determined at 2.3 A resolution. CyclinA binds to one side of CDK2's catalytic cleft, inducing large conformational changes in its PSTAIRE helix and T-loop. These changes activate the kinase by realigning active site residues and relieving the steric blockade at the entrance of the catalytic cleft. PubMed: 7630397DOI: 10.1038/376313a0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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