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1fpu
From Proteopedia
CRYSTAL STRUCTURE OF ABL KINASE DOMAIN IN COMPLEX WITH A SMALL MOLECULE INHIBITOR
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1FPU is a 2 chains structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
- Schindler T, Bornmann W, Pellicena P, Miller WT, Clarkson B, Kuriyan J. Structural mechanism for STI-571 inhibition of abelson tyrosine kinase. Science. 2000 Sep 15;289(5486):1938-42. PMID:10988075
Page seeded by OCA on Tue Feb 17 16:24:41 2009
