-
- Comment in:
-
Nature. 1995 Jul 27;376(6538):294-5.
Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex.
Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.
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.
PMID: 7630397 [PubMed - indexed for MEDLINE]
-
Cited by over 100 PubMed Central articles
-
3-D structure and dynamics of protein kinase B-new mechanism for the allosteric regulation of an AGC kinase.
Calleja V, Laguerre M, Larijani B.
J Chem Biol. 2009 Mar; 2(1):11-25. Epub 2009 Feb 20.
[J Chem Biol. 2009]
-
ATP and MO25alpha regulate the conformational state of the STRADalpha pseudokinase and activation of the LKB1 tumour suppressor.
Zeqiraj E, Filippi BM, Goldie S, Navratilova I, Boudeau J, Deak M, Alessi DR, van Aalten DM.
PLoS Biol. 2009 Jun 9; 7(6):e1000126. Epub 2009 Jun 9.
[PLoS Biol. 2009]
-
Distinct activation pathways confer cyclin-binding specificity on Cdk1 and Cdk2 in human cells.
Merrick KA, Larochelle S, Zhang C, Allen JJ, Shokat KM, Fisher RP.
Mol Cell. 2008 Dec 5; 32(5):662-72.
[Mol Cell. 2008]
- » See all...
Structures reported by this article