期刊
PROTEIN ENGINEERING DESIGN & SELECTION
卷 19, 期 8, 页码 345-353出版社
OXFORD UNIV PRESS
DOI: 10.1093/protein/gzl012
关键词
molecular modeling; cytochrome P450 monooxygenases; P450s
资金
- NIGMS NIH HHS [R01 GM71826] Funding Source: Medline
Different procedures for obtaining homology models for P450s are investigated using various sequence alignments sharing various levels of sequence identity with available P450 crystal structures. In this analysis, we have investigated how well homology modeling can reproduce known crystal structures as well as how effectively these homology models can be used to reproduce known ligand-binding modes. Homology models obtained from sequence alignments that discriminate between Class I and Class II P450s are significantly closer to the experimental crystal structures and more closely reproduce known ligand's binding modes, than those obtained using sequence alignments that combine Class I and Class II P450s. The quality of the models is slightly improved by constructing hybrid-structure models that model three of the most variable regions of P450s independently from the rest of the protein: the B region that includes SRS1, the FG region that includes SRS2 and SRS3 and the beta 4 region that includes SRS6.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据