Browse by author
Lookup NU author(s): Professor Martin NobleORCiD
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
The CDK-interacting protein phosphatase KAP dephosphorylates phosphoThr-160 (pThr-160) of the CDK2 activation segment, the site of regulatory phosphorylation that is essential for kinase activity. Here we describe the crystal structure of KAP in association with pThr-160-CDK2, representing an example of a protein phosphatase in complex with its intact protein substrate. The major protein interface between the two molecules is formed by the C-terminal lobe of CDK2 and the C-terminal helix of KAP, regions remote from the kinase-activation segment and the KAP catalytic site. The kinase-activation segment interacts with the catalytic site of KAP almost entirely via the phosphate group of pThr-160. This interaction requires that the activation segment is unfolded and drawn away from the kinase molecule, inducing a conformation of CDK2 similar to the activated state observed in the CDK2/cyclin A complex.
Author(s): Song HW, Hanlon N, Brown NR, Noble MEM, Johnson LN, Barford D
Publication type: Article
Publication status: Published
Journal: Molecular Cell
ISSN (print): 1097-2765
ISSN (electronic): 1097-4164
Publisher: Cell Press
Altmetrics provided by Altmetric