Nature Communications (Jan 2021)
Crystal structure of steroid reductase SRD5A reveals conserved steroid reduction mechanism
- Yufei Han,
- Qian Zhuang,
- Bo Sun,
- Wenping Lv,
- Sheng Wang,
- Qingjie Xiao,
- Bin Pang,
- Youli Zhou,
- Fuxing Wang,
- Pengliang Chi,
- Qisheng Wang,
- Zhen Li,
- Lizhe Zhu,
- Fuping Li,
- Dong Deng,
- Ying-Chih Chiang,
- Zhenfei Li,
- Ruobing Ren
Affiliations
- Yufei Han
- Kobilka Institute of Innovative Drug Discovery, School of Life and Health Sciences, The Chinese University of Hong Kong, Shenzhen
- Qian Zhuang
- State Key Laboratory of Cell Biology, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, University of Chinese Academy of Sciences
- Bo Sun
- Shanghai Synchrotron Radiation Facility, Shanghai Advanced Research Institute, Chinese Academy of Sciences
- Wenping Lv
- Warshel Institute for Computational Biology, School of Life and Health Sciences, The Chinese University of Hong Kong, Shenzhen
- Sheng Wang
- Tencent AI lab, Shenzhen
- Qingjie Xiao
- Department of Obstetrics, Key Laboratory of Birth Defects and Related Disease of Women and Children of MOE, State Key Laboratory of Biotherapy, West China Second Hospital, Sichuan University
- Bin Pang
- Kobilka Institute of Innovative Drug Discovery, School of Life and Health Sciences, The Chinese University of Hong Kong, Shenzhen
- Youli Zhou
- Kobilka Institute of Innovative Drug Discovery, School of Life and Health Sciences, The Chinese University of Hong Kong, Shenzhen
- Fuxing Wang
- Kobilka Institute of Innovative Drug Discovery, School of Life and Health Sciences, The Chinese University of Hong Kong, Shenzhen
- Pengliang Chi
- Department of Obstetrics, Key Laboratory of Birth Defects and Related Disease of Women and Children of MOE, State Key Laboratory of Biotherapy, West China Second Hospital, Sichuan University
- Qisheng Wang
- Shanghai Synchrotron Radiation Facility, Shanghai Advanced Research Institute, Chinese Academy of Sciences
- Zhen Li
- School of Science and Engineering, The Chinese University of Hong Kong, Shenzhen
- Lizhe Zhu
- Warshel Institute for Computational Biology, School of Life and Health Sciences, The Chinese University of Hong Kong, Shenzhen
- Fuping Li
- Human Sperm Bank, Key Laboratory of Birth Defects and Related Disease of Women and Children of MOE, West China Second Hospital, Sichuan University
- Dong Deng
- Department of Obstetrics, Key Laboratory of Birth Defects and Related Disease of Women and Children of MOE, State Key Laboratory of Biotherapy, West China Second Hospital, Sichuan University
- Ying-Chih Chiang
- Kobilka Institute of Innovative Drug Discovery, School of Life and Health Sciences, The Chinese University of Hong Kong, Shenzhen
- Zhenfei Li
- State Key Laboratory of Cell Biology, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, University of Chinese Academy of Sciences
- Ruobing Ren
- Kobilka Institute of Innovative Drug Discovery, School of Life and Health Sciences, The Chinese University of Hong Kong, Shenzhen
- DOI
- https://doi.org/10.1038/s41467-020-20675-2
- Journal volume & issue
-
Vol. 12,
no. 1
pp. 1 – 10
Abstract
Steroid 5α-reductase 2 (SRD5A2), a testosterone metabolism enzyme, is implicated in human disease. Structural and biochemical analyses of PbSRD5A, a bacterial homolog, reveal SRD5A2 substrate binding pocket and provide framework for the design of new drugs targeting this enzyme.
