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.
