Crystal structure of steroid reductase SRD5A reveals conserved steroid reduction mechanism

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.

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Autores principales:	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
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/020230f5b0f84fb48a87bd72d847fb71
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spelling	oai:doaj.org-article:020230f5b0f84fb48a87bd72d847fb712021-12-02T13:57:03ZCrystal structure of steroid reductase SRD5A reveals conserved steroid reduction mechanism10.1038/s41467-020-20675-22041-1723https://doaj.org/article/020230f5b0f84fb48a87bd72d847fb712021-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20675-2https://doaj.org/toc/2041-1723Steroid 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.Yufei HanQian ZhuangBo SunWenping LvSheng WangQingjie XiaoBin PangYouli ZhouFuxing WangPengliang ChiQisheng WangZhen LiLizhe ZhuFuping LiDong DengYing-Chih ChiangZhenfei LiRuobing RenNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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 Crystal structure of steroid reductase SRD5A reveals conserved steroid reduction mechanism
description	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.
format	article
author	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
author_facet	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
author_sort	Yufei Han
title	Crystal structure of steroid reductase SRD5A reveals conserved steroid reduction mechanism
title_short	Crystal structure of steroid reductase SRD5A reveals conserved steroid reduction mechanism
title_full	Crystal structure of steroid reductase SRD5A reveals conserved steroid reduction mechanism
title_fullStr	Crystal structure of steroid reductase SRD5A reveals conserved steroid reduction mechanism
title_full_unstemmed	Crystal structure of steroid reductase SRD5A reveals conserved steroid reduction mechanism
title_sort	crystal structure of steroid reductase srd5a reveals conserved steroid reduction mechanism
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/020230f5b0f84fb48a87bd72d847fb71
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Crystal structure of steroid reductase SRD5A reveals conserved steroid reduction mechanism

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