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Bioorg Med Chem Lett. 2009 Dec 1;19(23):6557-60. doi: 10.1016/j.bmcl.2009.10.038. Epub 2009 Oct 13.

Structural basis for the inhibitor recognition of human Lyn kinase domain.

Author information

1
Graduate School of Science, Osaka Prefecture University, Sakai, Osaka 599-8531, Japan.

Abstract

Human Lyn tyrosine kinase is expressed in hematopoietic tissues and plays crucial roles in the signal transduction of hematopoietic immune system. Its excess activity is involved in several tumors. The crystal structure has revealed that the potent inhibitor staurosporine binds to human Lyn kinase domain at the ATP-binding site. The remarkable structural features of the staurosporine-binding region will offer valuable structural insights for the structure-based design of novel Lyn-selective inhibitors.

PMID:
19857964
DOI:
10.1016/j.bmcl.2009.10.038
[Indexed for MEDLINE]

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