2v7a

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spinqualitylabelsall models 2v7a, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF THE T315I ABL MUTANT IN COMPLEX WITH THE INHIBITOR PHA-739358

Overview

Mutations in the kinase domain of Bcr-Abl are the most common cause of, resistance to therapy with imatinib in patients with chronic myelogenous, leukemia (CML). Second-generation Bcr-Abl inhibitors are able to overcome, most imatinib-resistant mutants, with the exception of the frequent T315I, substitution, which is emerging as a major cause of resistance to these, drugs in CML patients. Structural studies could be used to support the, drug design process for the development of inhibitors able to target the, T315I substitution, but until now no crystal structure of the T315I Abl, mutant has been solved. We show here the first crystal structure of the, kinase domain of Abl T315I in complex with PHA-739358, an Aurora kinase, inhibitor currently in clinical development for solid and ... [(full description)]

About this Structure

2V7A is a [Single protein] structure of sequence from [Homo sapiens] with MG and 627 as [ligands]. Active as [Non-specific protein-tyrosine kinase], with EC number [2.7.10.2]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Crystal Structure of the T315I Abl Mutant in Complex with the Aurora Kinases Inhibitor PHA-739358., Modugno M, Casale E, Soncini C, Rosettani P, Colombo R, Lupi R, Rusconi L, Fancelli D, Carpinelli P, Cameron AD, Isacchi A, Moll J, Cancer Res. 2007 Sep 1;67(17):7987-90. PMID:17804707

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