Docking Studies on the Interaction of Imidazolines and Potassium Ion Channel-Kir6.2

NWIPB OpenIR

	Docking Studies on the Interaction of Imidazolines and Potassium Ion Channel-Kir6.2
	Zhang Rui ; Ling Bao-Ping ; Meng Xiang-Hua ; Wang Zhi-Guo ; Zhang Chang-Qiao ; Liu Yong-Jun ; Liu Cheng-Bu
	2009-11-10
发表期刊	CHEMICAL JOURNAL OF CHINESE UNIVERSITIES-CHINESE ; Zhang, R; Ling, BP; Meng, XH; Wang, ZG; Zhang, CQ; Liu, YJ; Liu, CB.Docking Studies on the Interaction of Imidazolines and Potassium Ion Channel-Kir6.2,CHEMICAL JOURNAL OF CHINESE UNIVERSITIES-CHINESE,2009,30(11):2268-2273
摘要	Kir6.2, a key component of the ATP-sensitive potassium channel (K(ATP)), can directly interact with imidazolines, a kind of potential antidiabetic drug. This paper explored the interaction of Kir6.2 with imidazoline molecules by applying AutoDock software. The docking results reveal the binding sites of the seven imidazolines on Kir6.2. For Efaroxan, Clonidine, Cibenzoline and Bl1 1282, polar residues, H175, K67 and W68, constitute the binding pocket; while Rx871024, Alinidine and Ly389382, lies in a hydrophobic pocket which is composed of nonpolar residues, F168, M169 and 1296. Efaroxan, Clonidine, Cibenzoline and Bl1 1282 interact with Kir6.2 mainly by forming hydrogen bonds, but for Rx871024, Alinidine and Ly389382, the hydrophobic interaction is the most important mode of action. These binding sites and the interaction modes can interpret the inhibition of these imidazoline drugs to some extent, and this research may provide theoretical support in the pharmacological study of imidazolines regulating the secretion of insulin.; Kir6.2, a key component of the ATP-sensitive potassium channel (K(ATP)), can directly interact with imidazolines, a kind of potential antidiabetic drug. This paper explored the interaction of Kir6.2 with imidazoline molecules by applying AutoDock software. The docking results reveal the binding sites of the seven imidazolines on Kir6.2. For Efaroxan, Clonidine, Cibenzoline and Bl1 1282, polar residues, H175, K67 and W68, constitute the binding pocket; while Rx871024, Alinidine and Ly389382, lies in a hydrophobic pocket which is composed of nonpolar residues, F168, M169 and 1296. Efaroxan, Clonidine, Cibenzoline and Bl1 1282 interact with Kir6.2 mainly by forming hydrogen bonds, but for Rx871024, Alinidine and Ly389382, the hydrophobic interaction is the most important mode of action. These binding sites and the interaction modes can interpret the inhibition of these imidazoline drugs to some extent, and this research may provide theoretical support in the pharmacological study of imidazolines regulating the secretion of insulin.
文献类型	期刊论文
条目标识符	http://210.75.249.4/handle/363003/46044
专题	中国科学院西北高原生物研究所
推荐引用方式 GB/T 7714	Zhang Rui,Ling Bao-Ping,Meng Xiang-Hua,et al. Docking Studies on the Interaction of Imidazolines and Potassium Ion Channel-Kir6.2[J]. CHEMICAL JOURNAL OF CHINESE UNIVERSITIES-CHINESE, Zhang, R; Ling, BP; Meng, XH; Wang, ZG; Zhang, CQ; Liu, YJ; Liu, CB.Docking Studies on the Interaction of Imidazolines and Potassium Ion Channel-Kir6.2,CHEMICAL JOURNAL OF CHINESE UNIVERSITIES-CHINESE,2009,30(11):2268-2273,2009.
APA	Zhang Rui.,Ling Bao-Ping.,Meng Xiang-Hua.,Wang Zhi-Guo.,Zhang Chang-Qiao.,...&Liu Cheng-Bu.(2009).Docking Studies on the Interaction of Imidazolines and Potassium Ion Channel-Kir6.2.CHEMICAL JOURNAL OF CHINESE UNIVERSITIES-CHINESE.
MLA	Zhang Rui,et al."Docking Studies on the Interaction of Imidazolines and Potassium Ion Channel-Kir6.2".CHEMICAL JOURNAL OF CHINESE UNIVERSITIES-CHINESE (2009).