| A model of 3D-structure of H+, K+-ATPase catalytic subunit derived by homology modeling | |
| Alternative Title | A model of 3D-structure of H+, K+-ATPase catalytic subunit derived by homology modeling |
| Yan D1; Hu YD1; Li S1; Cheng MS1 | |
| 2004 | |
| Source Publication | ACTA PHARMACOLOGICA SINICA
 |
| ISSN | 1671-4083 |
| Volume | 25Issue:4Pages:474-479 |
| Abstract | AIM: To build a model of 3D-structure of H+, K+-ATPase catalytic subunit for theoretical study and anti-ulcer drug design. METHODS: The model was built on the basis of structural data from the Ca2+-ATPase. Structurally conserved regions were defined by amino acid sequence comparisons, optimum interconnecting loops were selected from the protein databank, and amino (N)- and carboxyl (C)-terminal ends were generated as random coil structures. Applying molecular mechanics method then minimized the model energy. Molecular dynamics technique was used to do further structural optimization. RESULTS: The model of 3D-structure of H+, K+-ATPase was derived. The model is reasonable according to several validation criteria. There were ten transmembrane helices (TM1-TM10) in the model and inhibitor-binding site was identified on the TM5-8 riched negatively charged residues. CONCLUSION: The 3D-structure model from our study is informative to guide future molecular biology study about H+, K+-ATPase and drug design based on database searching. |
| Other Abstract | AIM: To build a model of 3D-structure of H+, K+-ATPase catalytic subunit for theoretical study and anti-ulcer drug design. METHODS: The model was built on the basis of structural data from the Ca2+-ATPase. Structurally conserved regions were defined by amino acid sequence comparisons, optimum interconnecting loops were selected from the protein databank, and amino (N)- and carboxyl (C)-terminal ends were generated as random coil structures. Applying molecular mechanics method then minimized the model energy. Molecular dynamics technique was used to do further structural optimization. RESULTS: The model of 3D-structure of H+, K+-ATPase was derived. The model is reasonable according to several validation criteria. There were ten transmembrane helices (TM1-TM10) in the model and inhibitor-binding site was identified on the TM5-8 riched negatively charged residues. CONCLUSION: The 3D-structure model from our study is informative to guide future molecular biology study about H+, K+-ATPase and drug design based on database searching. |
| Keyword | GASTRIC H+/K+-ATPASE OMEPRAZOLE MEMBRANE TRANSPORT PUMP peptic ulcer H(+)-K(+)-exchanging ATPase protein structural homology drug design |
| Indexed By | CSCD |
| Language | 英语 |
| CSCD ID | CSCD:1842249 |
| Citation statistics | |
| Document Type | 期刊论文 |
| Identifier | http://ir.imr.ac.cn/handle/321006/142792 |
| Collection | 中国科学院金属研究所 |
| Affiliation | 1.Acad Mil Med Science 2.中国科学院金属研究所 |
| Recommended Citation GB/T 7714 | Yan D,Hu YD,Li S,et al. A model of 3D-structure of H+, K+-ATPase catalytic subunit derived by homology modeling[J]. ACTA PHARMACOLOGICA SINICA,2004,25(4):474-479. |
| APA | Yan D,Hu YD,Li S,&Cheng MS.(2004).A model of 3D-structure of H+, K+-ATPase catalytic subunit derived by homology modeling.ACTA PHARMACOLOGICA SINICA,25(4),474-479. |
| MLA | Yan D,et al."A model of 3D-structure of H+, K+-ATPase catalytic subunit derived by homology modeling".ACTA PHARMACOLOGICA SINICA 25.4(2004):474-479. |
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