Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
- 27 July 1995
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 376 (6538) , 313-320
- https://doi.org/10.1038/376313a0
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.Keywords
This publication has 47 references indexed in Scilit:
- The interpretation of protein structures: Estimation of static accessibilityPublished by Elsevier ,2004
- Differential regulation of E2F transactivation by cyclin/cdk2 complexes.Genes & Development, 1994
- Localization of Cyclin A at the Sites of Cellular DNA ReplicationExperimental Cell Research, 1993
- Purification and Crystallization of Human Cyclin-dependent Kinase 2Journal of Molecular Biology, 1993
- Maternal mRNA from clam oocytes can be specifically unmasked in vitro by antisense RNA complementary to the 3'-untranslated region.Genes & Development, 1990
- ANTIBODY-ANTIGEN COMPLEXESAnnual Review of Biochemistry, 1990
- CHAIN — A crystallographic modeling programJournal of Molecular Graphics, 1988
- Experiences with a new translation-function programJournal of Applied Crystallography, 1987
- An efficient general-purpose least-squares refinement program for macromolecular structuresActa Crystallographica Section A Foundations of Crystallography, 1987
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983