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Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
- Source :
- Nature. 376:313-320
- Publication Year :
- 1995
- Publisher :
- Springer Science and Business Media LLC, 1995.
-
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.
- Subjects :
- Threonine
Protein Folding
Protein Conformation
Stereochemistry
Molecular Sequence Data
Allosteric regulation
Protein Serine-Threonine Kinases
Crystallography, X-Ray
CDK-activating kinase
Adenosine Triphosphate
Protein structure
Allosteric Regulation
Cyclin-dependent kinase
Cyclins
CDC2-CDC28 Kinases
Computer Graphics
Escherichia coli
Humans
Amino Acid Sequence
Phosphorylation
Cyclin binding
Binding Sites
Multidisciplinary
biology
Chemistry
Cyclin-Dependent Kinase 2
Cyclin-dependent kinase 2
Active site
Cyclic AMP-Dependent Protein Kinases
Cyclin-Dependent Kinases
Recombinant Proteins
Enzyme Activation
biology.protein
Protein folding
sense organs
Protein Binding
Subjects
Details
- ISSN :
- 14764687 and 00280836
- Volume :
- 376
- Database :
- OpenAIRE
- Journal :
- Nature
- Accession number :
- edsair.doi.dedup.....1786a2dad1bc737d6580bbbb398cf35f