1FQ1

CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) IN COMPLEX WITH PHOSPHO-CDK2

Summary for 1FQ1

• Entry DOI: 10.2210/pdb1fq1/pdb
• Related: 1FPZ
• Descriptor: CYCLIN-DEPENDENT KINASE INHIBITOR 3, CELL DIVISION PROTEIN KINASE 2, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: phospho-protein-protein complex, hydrolase-transferase complex, hydrolase/transferase
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm, perinuclear region : Q16667; Cytoplasm, cytoskeleton, microtubule organizing center, centrosome: P24941
• Total number of polymer chains: 2
• Total formula weight: 58407.01

Authors

Song, H.,Hanlon, N.,Brown, N.R.,Noble, M.E.M.,Johnson, L.N.,Barford, D. (deposition date: 2000-09-01, release date: 2001-05-09, Last modification date: 2024-11-20)

Primary citation

Song, H.,Hanlon, N.,Brown, N.R.,Noble, M.E.,Johnson, L.N.,Barford, D.
Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2.
Mol.Cell, 7:615-626, 2001

PubMed Abstract: 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.

PubMed: 11463386
DOI: 10.1016/S1097-2765(01)00208-8

Experimental method

X-RAY DIFFRACTION (3 Å)