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
Dans Chinois
| 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.
Texte intégral:
Disponible
Indice:
WPRIM (Pacifique occidental)
Sujet Principal:
Pharmacologie
/
Modèles moléculaires
/
Génistéine
/
Domaine catalytique
/
Récepteurs ErbB
/
Métabolisme
Type d'étude:
Étude pronostique
langue:
Chinois
Texte intégral:
Chinese Journal of Biotechnology
Année:
2008
Type:
Article
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