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Structural analysis of recombinant human ubiquitin-conjugating enzyme UbcH5c
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作者 fangshu wu Junsheng Zhu +1 位作者 Honglin Li Lili Zhu 《Acta Pharmaceutica Sinica B》 SCIE CAS CSCD 2017年第3期390-394,共5页
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 t... 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. 展开更多
关键词 UbcH5c NF-ΚB UBIQUITINATION Ubiquitin-conjugating enzyme Crystal structure Inflammatory target
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