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

Article Details

Citation

Miyano N, Kinoshita T, Nakai R, Kirii Y, Yokota K, Tada T

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

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

PubMed ID
19857964 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Tyrosine-protein kinase LynP07948Details
Binding Properties
DrugTargetPropertyMeasurementpHTemperature (°C)
StaurosporineTyrosine-protein kinase LckIC 50 (nM)1.5N/AN/ADetails