1opj
From Proteopedia
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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
1OPJ is a Single protein structure of sequence from Mus musculus with CL, MYR and STI as ligands. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 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 Tue Nov 20 23:05:16 2007
Categories: Mus musculus | Single protein | Transferase | Bornmann, W. | Clarkson, B. | Hantschel, O. | Kuriyan, J. | Nagar, B. | Scheffzek, K. | Superti-Furga, G. | Veach, D. | Young, M.A. | CL | MYR | STI
