详细信息
Structural analysis of recombinant human ubiquitin-conjugating enzyme UbcH5c
文献类型:期刊文献
中文题名:Structural analysis of recombinant human ubiquitin-conjugating enzyme UbcH5c
英文题名:Structural analysis of recombinant human ubiquitin-conjugating enzyme UbcH5c
作者:Fangshu Wu[1];Junsheng Zhu[1];Honglin Li[1];Lili Zhu[1]
机构:[1]Shanghai Key Laboratory of New Drug Design,School of Pharmacy,East China University of Science and Technology,Shanghai 200237,China
年份:2017
卷号:7
期号:3
起止页码:390
中文期刊名:Acta Pharmaceutica Sinica B
外文期刊名:药学学报(英文版)
收录:CSTPCD;;Scopus;CSCD:【CSCD2017_2018】;PubMed;
基金:supported by the National Natural Science Foundation of China(grants 21372078,81302697 and 81230090);the National S&T Major Project of China(grant 2013ZX09507004);the Shanghai Committee of Science and Technology(grant 14431902400);the Fundamental Research Funds for the Central Universities
语种:英文
中文关键词:UbcH5c;NF-κB;Ubiquitination;Ubiquitin-conjugating enzyme;Crystal structure;Inflammatory target
外文关键词:UbcH5c;;NF-κB;;Ubiquitination;;Ubiquitin-conjugating enzyme;;Crystal structure;;Inflammatory target
摘要:UbcH5c belongs to the ubiquitin-conjugating enzyme family and plays an important role in catalyzing ubiquitination during TNF-α–triggered NF-κB activation. Therefore, UbcH5c is a potent therapeutic target for the treatment of inflammatory and autoimmune diseases induced by aberrant activation of NF-κB. In this study, we established a stable expression system for recombinant UbcH5c and solved the crystal structure of UbcH5c belonging to space group P22_12_1 with one molecule in the asymmetric unit. This study provides the basis for further study of UbcH5c including the design of UbcH5c inhibitors.
UbcH5c belongs to the ubiquitin-conjugating enzyme family and plays an important role in catalyzing ubiquitination during TNF-α–triggered NF-κB activation. Therefore, UbcH5c is a potent therapeutic target for the treatment of inflammatory and autoimmune diseases induced by aberrant activation of NF-κB. In this study, we established a stable expression system for recombinant UbcH5c and solved the crystal structure of UbcH5c belonging to space group P22_12_1 with one molecule in the asymmetric unit. This study provides the basis for further study of UbcH5c including the design of UbcH5c inhibitors.
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