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.
Autor*in: |
Yufei Han [verfasserIn] Qian Zhuang [verfasserIn] Bo Sun [verfasserIn] Wenping Lv [verfasserIn] Sheng Wang [verfasserIn] Qingjie Xiao [verfasserIn] Bin Pang [verfasserIn] Youli Zhou [verfasserIn] Fuxing Wang [verfasserIn] Pengliang Chi [verfasserIn] Qisheng Wang [verfasserIn] Zhen Li [verfasserIn] Lizhe Zhu [verfasserIn] Fuping Li [verfasserIn] Dong Deng [verfasserIn] Ying-Chih Chiang [verfasserIn] Zhenfei Li [verfasserIn] Ruobing Ren [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2021 |
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Übergeordnetes Werk: |
In: Nature Communications - Nature Portfolio, 2016, 12(2021), 1, Seite 10 |
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Übergeordnetes Werk: |
volume:12 ; year:2021 ; number:1 ; pages:10 |
Links: |
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DOI / URN: |
10.1038/s41467-020-20675-2 |
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Katalog-ID: |
DOAJ052576922 |
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10.1038/s41467-020-20675-2 doi (DE-627)DOAJ052576922 (DE-599)DOAJ020230f5b0f84fb48a87bd72d847fb71 DE-627 ger DE-627 rakwb eng Yufei Han verfasserin aut Crystal structure of steroid reductase SRD5A reveals conserved steroid reduction mechanism 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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. Science Q Qian Zhuang verfasserin aut Bo Sun verfasserin aut Wenping Lv verfasserin aut Sheng Wang verfasserin aut Qingjie Xiao verfasserin aut Bin Pang verfasserin aut Youli Zhou verfasserin aut Fuxing Wang verfasserin aut Pengliang Chi verfasserin aut Qisheng Wang verfasserin aut Zhen Li verfasserin aut Lizhe Zhu verfasserin aut Fuping Li verfasserin aut Dong Deng verfasserin aut Ying-Chih Chiang verfasserin aut Zhenfei Li verfasserin aut Ruobing Ren verfasserin aut In Nature Communications Nature Portfolio, 2016 12(2021), 1, Seite 10 (DE-627)626457688 (DE-600)2553671-0 20411723 nnns volume:12 year:2021 number:1 pages:10 https://doi.org/10.1038/s41467-020-20675-2 kostenfrei https://doaj.org/article/020230f5b0f84fb48a87bd72d847fb71 kostenfrei https://doi.org/10.1038/s41467-020-20675-2 kostenfrei https://doaj.org/toc/2041-1723 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_211 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2110 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2021 1 10 |
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10.1038/s41467-020-20675-2 doi (DE-627)DOAJ052576922 (DE-599)DOAJ020230f5b0f84fb48a87bd72d847fb71 DE-627 ger DE-627 rakwb eng Yufei Han verfasserin aut Crystal structure of steroid reductase SRD5A reveals conserved steroid reduction mechanism 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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. Science Q Qian Zhuang verfasserin aut Bo Sun verfasserin aut Wenping Lv verfasserin aut Sheng Wang verfasserin aut Qingjie Xiao verfasserin aut Bin Pang verfasserin aut Youli Zhou verfasserin aut Fuxing Wang verfasserin aut Pengliang Chi verfasserin aut Qisheng Wang verfasserin aut Zhen Li verfasserin aut Lizhe Zhu verfasserin aut Fuping Li verfasserin aut Dong Deng verfasserin aut Ying-Chih Chiang verfasserin aut Zhenfei Li verfasserin aut Ruobing Ren verfasserin aut In Nature Communications Nature Portfolio, 2016 12(2021), 1, Seite 10 (DE-627)626457688 (DE-600)2553671-0 20411723 nnns volume:12 year:2021 number:1 pages:10 https://doi.org/10.1038/s41467-020-20675-2 kostenfrei https://doaj.org/article/020230f5b0f84fb48a87bd72d847fb71 kostenfrei https://doi.org/10.1038/s41467-020-20675-2 kostenfrei https://doaj.org/toc/2041-1723 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_211 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2110 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2021 1 10 |
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10.1038/s41467-020-20675-2 doi (DE-627)DOAJ052576922 (DE-599)DOAJ020230f5b0f84fb48a87bd72d847fb71 DE-627 ger DE-627 rakwb eng Yufei Han verfasserin aut Crystal structure of steroid reductase SRD5A reveals conserved steroid reduction mechanism 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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. Science Q Qian Zhuang verfasserin aut Bo Sun verfasserin aut Wenping Lv verfasserin aut Sheng Wang verfasserin aut Qingjie Xiao verfasserin aut Bin Pang verfasserin aut Youli Zhou verfasserin aut Fuxing Wang verfasserin aut Pengliang Chi verfasserin aut Qisheng Wang verfasserin aut Zhen Li verfasserin aut Lizhe Zhu verfasserin aut Fuping Li verfasserin aut Dong Deng verfasserin aut Ying-Chih Chiang verfasserin aut Zhenfei Li verfasserin aut Ruobing Ren verfasserin aut In Nature Communications Nature Portfolio, 2016 12(2021), 1, Seite 10 (DE-627)626457688 (DE-600)2553671-0 20411723 nnns volume:12 year:2021 number:1 pages:10 https://doi.org/10.1038/s41467-020-20675-2 kostenfrei https://doaj.org/article/020230f5b0f84fb48a87bd72d847fb71 kostenfrei https://doi.org/10.1038/s41467-020-20675-2 kostenfrei https://doaj.org/toc/2041-1723 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_211 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2110 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2021 1 10 |
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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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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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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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