Structural basis for the inhibitor recognition of human Lyn kinase domain.
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.
Miyano
Nao
N
Graduate School of Science, Osaka Prefecture University, Sakai, Osaka 599-8531, Japan.
Kinoshita
Takayoshi
T
Nakai
Ryoko
R
Kirii
Yasuyuki
Y
Yokota
Koichi
K
Tada
Toshiji
T
D001665:Binding Sites; D018360:Crystallography, X-Ray; D015195:Drug Design; D006801:Humans; D008958:Models, Molecular; D015394:Molecular Structure; D047428:Protein Kinase Inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D019311:Staurosporine / Q000737:chemistry* / Q000494:pharmacology*; D013329:Structure-Activity Relationship; D019061:src-Family Kinases / Q000037:antagonists & inhibitors* / Q000737:chemistry*
D047428:Protein Kinase Inhibitors; C060902:lyn protein-tyrosine kinase; D019061:src-Family Kinases; D019311:Staurosporine