[Molecular docking of epidermal growth factor receptor tyramine kinase domain and its inhibitor genistein].
Genistein is a high specific and noncompetitive inhibitor of epidermal growth factor receptor tyramine kinase domain (EGFR-TK). In the paper, a molecular docking between genistein and EGFR-TK was studied to explore the mechanism of their interaction and antitumor mechanism of genistein by AUTODOCK 3.05 program. The results indicated that genistein located in the active cavity of EGFR-TK by high affinity (deltaG = -31.2 kJ/mol), and genistein inhibited EGFR-TK by interfering with forming of Lys721/Glu738 ion pair. The inhibition belonged to noncompetitive interaction, in which hydrophobic force and hydrogen bond played key roles.
Yuan
Jianglan
J
College of Biological Engineering, Hubei University of Technology, Wuhan 430064, China. jlyuan1229@163.com
Liu
Hui
H
Kang
Xu
X
Zou
Guolin
G
D020134:Catalytic Domain; D066246:ErbB Receptors / Q000037:antagonists & inhibitors* / Q000378:metabolism; D019833:Genistein / Q000378:metabolism / Q000494:pharmacology*; D008958:Models, Molecular
D019833:Genistein; D066246:ErbB Receptors