Molecular docking of epidermal growth factor receptor tyramine kinase domain and its inhibitor genistein.
- Author:
Jianglan YUAN
1
;
Hui LIU
;
Xu KANG
;
Guolin ZOU
Author Information
1. College of Biological Engineering, Hubei University of Technology, Wuhan 430064, China. jlyuan1229@163.com
- Publication Type:Journal Article
- MeSH:
Catalytic Domain;
Genistein;
metabolism;
pharmacology;
Models, Molecular;
Receptor, Epidermal Growth Factor;
antagonists & inhibitors;
metabolism
- From:
Chinese Journal of Biotechnology
2008;24(10):1813-1817
- CountryChina
- Language:Chinese
-
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.
