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Molecular docking of epidermal growth factor receptor tyramine kinase domain and its inhibitor genistein / 生物工程学报
Chinese Journal of Biotechnology ; (12): 1813-1817, 2008.
Article in Chinese | WPRIM | ID: wpr-275335
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.
Subject(s)
Full text: Available Index: WPRIM (Western Pacific) Main subject: Pharmacology / Models, Molecular / Genistein / Catalytic Domain / ErbB Receptors / Metabolism Type of study: Prognostic study Language: Chinese Journal: Chinese Journal of Biotechnology Year: 2008 Type: Article

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Full text: Available Index: WPRIM (Western Pacific) Main subject: Pharmacology / Models, Molecular / Genistein / Catalytic Domain / ErbB Receptors / Metabolism Type of study: Prognostic study Language: Chinese Journal: Chinese Journal of Biotechnology Year: 2008 Type: Article