Structural analysis of recombinant human ubiquitin-conjugating enzyme UbcH5c

Fangshu Wu; Junsheng Zhu; Honglin Li; Lili Zhu

doi:10.1016/j.apsb.2016.12.008

Structural analysis of recombinant human ubiquitin-conjugating enzyme UbcH5c

Fangshu Wu, Junsheng Zhu, Honglin Li, Lili Zhu

East China University of Science and Technology

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

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 P22₁2₁ with one molecule in the asymmetric unit. This study provides the basis for further study of UbcH5c including the design of UbcH5c inhibitors.

Original language	English
Pages (from-to)	390-394
Number of pages	5
Journal	Acta Pharmaceutica Sinica B
Volume	7
Issue number	3
DOIs	https://doi.org/10.1016/j.apsb.2016.12.008
State	Published - May 2017
Externally published	Yes

Keywords

Crystal structure
Inflammatory target
NF-κB
UbcH5c
Ubiquitin-conjugating enzyme
Ubiquitination

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10.1016/j.apsb.2016.12.008

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title = "Structural analysis of recombinant human ubiquitin-conjugating enzyme UbcH5c",

abstract = "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 P22121 with one molecule in the asymmetric unit. This study provides the basis for further study of UbcH5c including the design of UbcH5c inhibitors.",

keywords = "Crystal structure, Inflammatory target, NF-κB, UbcH5c, Ubiquitin-conjugating enzyme, Ubiquitination",

author = "Fangshu Wu and Junsheng Zhu and Honglin Li and Lili Zhu",

note = "Publisher Copyright: {\textcopyright} 2017 Chinese Pharmaceutical Association and Institute of Materia Medica, Chinese Academy of Medical Sciences",

year = "2017",

month = may,

doi = "10.1016/j.apsb.2016.12.008",

language = "英语",

volume = "7",

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journal = "Acta Pharmaceutica Sinica B",

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T1 - Structural analysis of recombinant human ubiquitin-conjugating enzyme UbcH5c

AU - Wu, Fangshu

AU - Zhu, Junsheng

AU - Li, Honglin

AU - Zhu, Lili

PY - 2017/5

Y1 - 2017/5

N2 - 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 P22121 with one molecule in the asymmetric unit. This study provides the basis for further study of UbcH5c including the design of UbcH5c inhibitors.

AB - 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 P22121 with one molecule in the asymmetric unit. This study provides the basis for further study of UbcH5c including the design of UbcH5c inhibitors.

KW - Crystal structure

KW - Inflammatory target

KW - NF-κB

KW - UbcH5c

KW - Ubiquitin-conjugating enzyme

KW - Ubiquitination

UR - https://www.scopus.com/pages/publications/85014003400

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DO - 10.1016/j.apsb.2016.12.008

M3 - 文章

AN - SCOPUS:85014003400

SN - 2211-3835

VL - 7

SP - 390

EP - 394

JO - Acta Pharmaceutica Sinica B

JF - Acta Pharmaceutica Sinica B

IS - 3

ER -

Structural analysis of recombinant human ubiquitin-conjugating enzyme UbcH5c

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Keywords

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