1opk: Difference between revisions

Revision as of 05:43, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1opk.png

Template:STRUCTURE 1opk

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

Template:ABSTRACT PUBMED 12654251

About this StructureAbout this Structure

1OPK is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

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

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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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===
-==Overview==
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-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.
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+{{ABSTRACT_PUBMED_12654251}}
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 [[Category: Young, M A.]]
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