Modeling of alpha k/gamma 2 (k = 1, 2, 3 and 5) interface of GABAA receptor and docking studies with zolpidem: Implications for selectivity
文献类型：期刊论文
| 作者 | Ci, Su-Qin; Ren, Tian-Rui; Ma, Cai-Xia; Su, Zhi-Guo |
| 刊名 | JOURNAL OF MOLECULAR GRAPHICS & MODELLING
 |
| 出版日期 | 2007-09-01 |
| 卷号 | 26期号:2页码:537-545 |
| 关键词 | alpha k/gamma 2 interface homology modeling zolpidem docking study selectivity |
| ISSN号 | 1093-3263 |
| 其他题名 | J. Mol. Graph. |
| 中文摘要 | The three-dimensional models of the alpha k/gamma 2 (k = 1, 2, 3 and 5) interface of GABA(A) receptors, which included the agonist-binding site, were constructed and validated by molecular modeling technology. To investigate the mechanism of a subunit selectivity of zolpidem, docking calculations were used to illustrate the potential binding modes of zolpidem with different a subtypes. The results revealed that there were three reasons resulting in the distinct binding affinity of zolpidem to different alpha subtype. Firstly, the number of hydrogen bonds of agonist-receptor complex would determine the magnitude of binding affinity. Secondly, the His residue in loop A of a subunit was indicated as a key role of benzodiazepine binding. Thirdly, the side chain of Glu in loop C reduced the affinity of zolpidem to those receptors containing alpha 2, alpha 3 or alpha 5 subunits. (c) 2007 Elsevier Inc. All rights reserved. |
| 英文摘要 | The three-dimensional models of the alpha k/gamma 2 (k = 1, 2, 3 and 5) interface of GABA(A) receptors, which included the agonist-binding site, were constructed and validated by molecular modeling technology. To investigate the mechanism of a subunit selectivity of zolpidem, docking calculations were used to illustrate the potential binding modes of zolpidem with different a subtypes. The results revealed that there were three reasons resulting in the distinct binding affinity of zolpidem to different alpha subtype. Firstly, the number of hydrogen bonds of agonist-receptor complex would determine the magnitude of binding affinity. Secondly, the His residue in loop A of a subunit was indicated as a key role of benzodiazepine binding. Thirdly, the side chain of Glu in loop C reduced the affinity of zolpidem to those receptors containing alpha 2, alpha 3 or alpha 5 subunits. (c) 2007 Elsevier Inc. All rights reserved. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine ; Technology ; Physical Sciences |
| 类目[WOS] | Biochemical Research Methods ; Biochemistry & Molecular Biology ; Computer Science, Interdisciplinary Applications ; Crystallography ; Mathematical & Computational Biology |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Computer Science ; Crystallography ; Mathematical & Computational Biology |
| 关键词[WOS] | AMINOBUTYRIC ACID(A) RECEPTORS ; BENZODIAZEPINE BINDING-SITE ; GATED ION CHANNELS ; NICOTINIC RECEPTORS ; AGONIST-BINDING ; ALPHA-SUBUNIT ; ACETYLCHOLINE-RECEPTOR ; GAP PENALTIES ; FORCE-FIELD ; PROTEIN |
| 收录类别 | SCI |
| 原文出处 | |
| 语种 | 英语 |
| WOS记录号 | WOS:000250182400015 |
| 公开日期 | 2013-10-15 |
| 版本 | 出版稿 |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/3300]  |
| 专题 | 过程工程研究所_研究所（批量导入） |
| 作者单位 | 1.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100080, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China |
| 推荐引用方式 GB/T 7714 | Ci, Su-Qin,Ren, Tian-Rui,Ma, Cai-Xia,et al. Modeling of alpha k/gamma 2 (k = 1, 2, 3 and 5) interface of GABAA receptor and docking studies with zolpidem: Implications for selectivity[J]. JOURNAL OF MOLECULAR GRAPHICS & MODELLING,2007,26(2):537-545. |
| APA | Ci, Su-Qin,Ren, Tian-Rui,Ma, Cai-Xia,&Su, Zhi-Guo.(2007).Modeling of alpha k/gamma 2 (k = 1, 2, 3 and 5) interface of GABAA receptor and docking studies with zolpidem: Implications for selectivity.JOURNAL OF MOLECULAR GRAPHICS & MODELLING,26(2),537-545. |
| MLA | Ci, Su-Qin,et al."Modeling of alpha k/gamma 2 (k = 1, 2, 3 and 5) interface of GABAA receptor and docking studies with zolpidem: Implications for selectivity".JOURNAL OF MOLECULAR GRAPHICS & MODELLING 26.2(2007):537-545. |
入库方式： OAI收割
来源：过程工程研究所
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