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A model of 3D-structure of H+, K+-ATPase catalytic subunit derived by homology modeling
Alternative TitleA model of 3D-structure of H+, K+-ATPase catalytic subunit derived by homology modeling
Yan D1; Hu YD1; Li S1; Cheng MS1
2004
Source PublicationACTA PHARMACOLOGICA SINICA
ISSN1671-4083
Volume25Issue:4Pages:474-479
AbstractAIM: 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 AbstractAIM: 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.
KeywordGASTRIC H+/K+-ATPASE OMEPRAZOLE MEMBRANE TRANSPORT PUMP peptic ulcer H(+)-K(+)-exchanging ATPase protein structural homology drug design
Indexed ByCSCD
Language英语
CSCD IDCSCD:1842249
Citation statistics
Document Type期刊论文
Identifierhttp://ir.imr.ac.cn/handle/321006/142792
Collection中国科学院金属研究所
Affiliation1.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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