2cjm

From Proteopedia

Revision as of 16:06, 5 November 2007

MECHANISM OF CDK INHIBITION BY ACTIVE SITE PHOSPHORYLATION: CDK2 Y15P T160P IN COMPLEX WITH CYCLIN A STRUCTURE

Overview

Inhibition of cyclin-dependent kinase 1 (CDK1) activity by Tyr-15, phosphorylation directly regulates entry into mitosis and is an important, element in the control of the unperturbed cell cycle. Active site, phosphorylation of other members of the CDK family that regulate cell, cycle progression instates checkpoints that are fundamental to eukaryotic, cell cycle regulation. Kinetic and crystallographic analyses of, CDK2-cyclin A complexes reveal that this inhibitory mechanism operates, through steric blockade of peptide substrate binding and through the, creation of an environment that favors a non-productive conformation of, the terminal group of ATP. By contrast, tyrosine phosphorylation of CDK2, alters neither its Km for ATP nor its significant intrinsic ATPase, activity. Tyr-15-phosphorylated CDK2 retains trace protein phosphorylation, activity that should be considered in quantitative and qualitative cell, cycle models.

About this Structure

2CJM is a Protein complex structure of sequences from Homo sapiens with MG, PTR and ATP as ligands. Active as Transferred entry: 2.7.11.1, with EC number 2.7.1.37 Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

How tyrosine 15 phosphorylation inhibits the activity of cyclin-dependent kinase 2-cyclin A., Welburn JP, Tucker JA, Johnson T, Lindert L, Morgan M, Willis A, Noble ME, Endicott JA, J Biol Chem. 2007 Feb 2;282(5):3173-81. Epub 2006 Nov 9. PMID:17095507

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