Docking Studies on the Interaction of Imidazolines and Potassium Ion Channel-Kir6.2
文献类型：期刊论文
| 作者 | Zhang Rui1,2,3; Ling Bao-Ping2; Meng Xiang-Hua2; Wang Zhi-Guo1,3; Zhang Chang-Qiao2; Liu Yong-Jun1,2; Liu Cheng-Bu2 |
| 刊名 | chemical journal of chinese universities-chinese
 |
| 出版日期 | 2009-11-10 |
| 卷号 | 30期号:11页码:2268-2273 |
| 关键词 | Imidazolines K(ATP) channel Kir6.2 Docking Binding site |
| ISSN号 | 0251-0790 |
| 中文摘要 | 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. |
| 英文摘要 | 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. |
| WOS标题词 | science & technology ; physical sciences |
| 类目[WOS] | chemistry, multidisciplinary |
| 研究领域[WOS] | chemistry |
| 关键词[WOS] | functional-analysis ; binding ; kir6.2 ; inhibitors ; channels ; site |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000272832200032 |
| 公开日期 | 2011-12-13 |
| 源URL | [http://ir.nwipb.ac.cn//handle/363003/1808]  |
| 专题 | 西北高原生物研究所_中国科学院西北高原生物研究所 |
| 作者单位 | 1.Chinese Acad Sci, NW Inst Plateau Biol, Xining 810001, Peoples R China 2.Shandong Univ, Sch Chem & Chem Engn, Jinan 250100, Peoples R China 3.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China |
| 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,2009,30(11):2268-2273. |
| 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,30(11),2268-2273. |
| MLA | Zhang Rui,et al."Docking Studies on the Interaction of Imidazolines and Potassium Ion Channel-Kir6.2".chemical journal of chinese universities-chinese 30.11(2009):2268-2273. |
入库方式： OAI收割
来源：西北高原生物研究所
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