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2ogv

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Revision as of 13:25, 23 January 2008 by OCA (Talk | contribs)
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2ogv, resolution 2.70Å

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Crystal Structure of the Autoinhibited Human c-Fms Kinase Domain

Overview

c-Fms, a member of the Platelet-derived Growth Factor (PDGF) receptor, family of receptor tyrosine kinases (RTKs), is the receptor for macrophage, colony stimulating factor (CSF-1) that regulates proliferation, differentiation and survival of cells of the mononuclear phagocyte, lineage. Abnormal expression of c-fms proto-oncogene is associated with a, significant number of human pathologies, including a variety of cancers, and rheumatoid arthritis. Accordingly, c-Fms represents an attractive, therapeutic target. To further understand the regulation of c-Fms, we, determined the 2.7 A resolution crystal structure of the cytosolic domain, of c-Fms that comprised the kinase domain and the juxtamembrane domain., The structure reveals the crucial inhibitory role of the juxtamembrane, domain (JM) that binds to a hydrophobic site immediately adjacent to the, ATP binding pocket. This interaction prevents the activation loop from, adopting an active conformation thereby locking the c-Fms kinase into an, autoinhibited state. As observed for other members of the PDGF receptor, family, namely c-Kit and Flt3, three JM-derived tyrosine residues, primarily drive the mechanism for autoinhibition in c-Fms, therefore, defining a common autoinhibitory mechanism within this family. Moreover, the structure provides an understanding of c-Fms inhibition by Gleevec as, well as providing a platform for the development of more selective, inhibitors that target the inactive conformation of c-Fms kinase.

About this Structure

2OGV is a Single protein structure of sequence from Homo sapiens. Active as Receptor protein-tyrosine kinase, with EC number 2.7.10.1 Full crystallographic information is available from OCA.

Reference

The 2.7 A crystal structure of the autoinhibited human c-Fms kinase domain., Walter M, Lucet IS, Patel O, Broughton SE, Bamert R, Williams NK, Fantino E, Wilks AF, Rossjohn J, J Mol Biol. 2007 Mar 30;367(3):839-47. Epub 2007 Jan 20. PMID:17292918

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