Structural basis for the inhibitor recognition of human Lyn kinase domain.
Article Details
- CitationCopy to clipboard
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
Name UniProt ID Tyrosine-protein kinase Lyn P07948 Details - Binding Properties
Drug Target Property Measurement pH Temperature (°C) Staurosporine Tyrosine-protein kinase Lck IC 50 (nM) 1.5 N/A N/A Details