Modeling Steroid 5alpha-reductase and Characterizing Its Potential Active Sites

• 作者: LI Jun-Qian OU Min-Rui
• 来源期刊: 结构化学
• 学科: 农学
• 关键词: 5α-还原酶 活性位点 同源建模 类固醇 特性 生物合成途径 对接技术 评估模型
• 年，卷（期）: 2012,（11）
• 页码范围: 1618-1626
• 页数: 9页
• 分类号: Q554|S435.111
• 语种: 英文

摘要

Steroid 5alpha-reductase of human is an enzyme in the biosynthetic pathway from testosterone (T) to dihydrotestosterone (DHT). Up to now, no crystal structure of this enzyme has been reported. However, knowledge of the tertiary structure and possible active sites is essential for understanding the catalysis mechanism and for the design of inhibitors. A model with putative active sites has been created and evaluated by using homology modeling and molecular docking techniques based on the bioinformatics knowledge. The homology model is optimized in Swiss PDB Viewer with MM method and substrate structures before docking are also optimized on HF/6-31G. The active site for the docking of NADP, T, DHT and Finasteride is located near the N-terminus of enzyme. Four active amino acids in the active site are identified as Ala26, Arg53, Arg176 and Lys177. Reaction procedure, binding pattern of active sites, the types of weak interaction and so on are also discussed.

作者信息

序号	姓名	单位	发文数	被引次数	H指数	G指数
1	OU Min-Rui		2	0	0.0	0.0
2	LI Jun-Qian		2	0	0.0	0.0