2cn5

From Proteopedia

Revision as of 15:08, 30 October 2007

CRYSTAL STRUCTURE OF HUMAN CHK2 IN COMPLEX WITH ADP

Overview

The protein kinase Chk2 (checkpoint kinase 2) is a major effector of the, replication checkpoint. Chk2 activation is initiated by phosphorylation of, Thr68, in the serine-glutamine/threonine-glutamine cluster domain (SCD), by ATM. The phosphorylated SCD-segment binds to the FHA domain of a second, Chk2 molecule, promoting dimerisation of the protein and triggering, phosphorylation of the activation segment/T-loop in the kinase domain. We, have now determined the structure of the kinase domain of human Chk2 in, complexes with ADP and a small-molecule inhibitor debromohymenialdisine., The structure reveals a remarkable dimeric arrangement in which T-loops, are exchanged between protomers, to form an active kinase conformation in, trans. Biochemical data suggest that this dimer is the ... [(full description)]

About this Structure

2CN5 is a [Single protein] structure of sequence from [Homo sapiens] with CL, MG, NO3 and ADP as [ligands]. Active as [Non-specific serine/threonine protein kinase], with EC number [2.7.11.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Trans-activation of the DNA-damage signalling protein kinase Chk2 by T-loop exchange., Oliver AW, Paul A, Boxall KJ, Barrie SE, Aherne GW, Garrett MD, Mittnacht S, Pearl LH, EMBO J. 2006 Jul 12;25(13):3179-90. Epub 2006 Jun 22. PMID:16794575

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