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1opl

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Revision as of 11:14, 20 March 2008 by OCA (Talk | contribs)
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PDB ID 1opl

Drag the structure with the mouse to rotate
, resolution 3.42Å
Ligands: and
Gene: Abl (Homo sapiens)
Activity: Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2
Coordinates: save as pdb, mmCIF, xml



Structural basis for the auto-inhibition of c-Abl tyrosine kinase


Contents

Overview

c-Abl is normally regulated by an autoinhibitory mechanism, the disruption of which leads to chronic myelogenous leukemia. The details of this mechanism have been elusive because c-Abl lacks a phosphotyrosine residue that triggers the assembly of the autoinhibited form of the closely related Src kinases by internally engaging the SH2 domain. Crystal structures of c-Abl show that the N-terminal myristoyl modification of c-Abl 1b binds to the kinase domain and induces conformational changes that allow the SH2 and SH3 domains to dock onto it. Autoinhibited c-Abl forms an assembly that is strikingly similar to that of inactive Src kinases but with specific differences that explain the differential ability of the drug STI-571/Gleevec/imatinib (STI-571) to inhibit the catalytic activity of Abl, but not that of c-Src.

Disease

Known diseases associated with this structure: Leukemia, Philadelphia chromosome-positive, resistant to imatinib OMIM:[189980]

About this Structure

1OPL is a Single protein structure of sequence from Homo sapiens. The following page contains interesting information on the relation of 1OPL with [Src Tyrosine Kinase]. Full crystallographic information is available from OCA.

Reference

Structural basis for the autoinhibition of c-Abl tyrosine kinase., Nagar B, Hantschel O, Young MA, Scheffzek K, Veach D, Bornmann W, Clarkson B, Superti-Furga G, Kuriyan J, Cell. 2003 Mar 21;112(6):859-71. PMID:12654251

Page seeded by OCA on Thu Mar 20 13:13:59 2008

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