1opl
From Proteopedia
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[[Image:1opl.jpg|left|200px]] | [[Image:1opl.jpg|left|200px]] | ||
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'''Structural basis for the auto-inhibition of c-Abl tyrosine kinase''' | '''Structural basis for the auto-inhibition of c-Abl tyrosine kinase''' | ||
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[[Category: Veach, D.]] | [[Category: Veach, D.]] | ||
[[Category: Young, M A.]] | [[Category: Young, M A.]] | ||
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Revision as of 01:08, 3 May 2008
Structural basis for the auto-inhibition of c-Abl tyrosine kinase
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.
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 Sat May 3 04:08:04 2008