title: [Molecular docking of epidermal growth factor receptor tyramine kinase domain and its inhibitor genistein].
abstract: 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.
authors.affiliation: College of Biological Engineering, Hubei University of Technology, Wuhan 430064, China. jlyuan1229@163.com
authors.forename: Jianglan
authors.initials: J
authors.lastname: Yuan
authors.forename: Hui
authors.initials: H
authors.lastname: Liu
authors.forename: Xu
authors.initials: X
authors.lastname: Kang
authors.forename: Guolin
authors.initials: G
authors.lastname: Zou
mesh_terms: D020134:Catalytic Domain; D066246:ErbB Receptors / Q000037:antagonists & inhibitors* / Q000378:metabolism; D019833:Genistein / Q000378:metabolism / Q000494:pharmacology*; D008958:Models, Molecular
chemical_list: D019833:Genistein; D066246:ErbB Receptors