1fpu
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(New page: 200px<br /><applet load="1fpu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fpu, resolution 2.4Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 13:00, 20 November 2007
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CRYSTAL STRUCTURE OF ABL KINASE DOMAIN IN COMPLEX WITH A SMALL MOLECULE INHIBITOR
Overview
The inadvertent activation of the Abelson tyrosine kinase (Abl) causes, chronic myelogenous leukemia (CML). A small-molecule inhibitor of Abl, (STI-571) is effective in the treatment of CML. We report the crystal, structure of the catalytic domain of Abl, complexed to a variant of, STI-571. Critical to the binding of STI-571 is the adoption by the kinase, of an inactive conformation, in which a centrally located "activation, loop" is not phosphorylated. The conformation of this loop is distinct, from that in active protein kinases, as well as in the inactive form of, the closely related Src kinases. These results suggest that compounds that, exploit the distinctive inactivation mechanisms of individual protein, kinases can achieve both high affinity and high specificity.
About this Structure
1FPU is a Single protein structure of sequence from Mus musculus with PRC as ligand. 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 mechanism for STI-571 inhibition of abelson tyrosine kinase., Schindler T, Bornmann W, Pellicena P, Miller WT, Clarkson B, Kuriyan J, Science. 2000 Sep 15;289(5486):1938-42. PMID:10988075
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