Structural analysis of recombinant human ubiquitin-conjugating enzyme UbcH5c
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...
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Format: | Article |
Language: | English |
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Elsevier
2017-05-01
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Series: | Acta Pharmaceutica Sinica B |
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Online Access: | http://www.sciencedirect.com/science/article/pii/S2211383516303677 |
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author | Fangshu Wu Junsheng Zhu Honglin Li Lili Zhu |
author_facet | Fangshu Wu Junsheng Zhu Honglin Li Lili Zhu |
author_sort | Fangshu Wu |
collection | DOAJ |
description | 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. |
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format | Article |
id | doaj.art-ba3edd839311499e977dcdc7fbc8f9f9 |
institution | Directory Open Access Journal |
issn | 2211-3835 2211-3843 |
language | English |
last_indexed | 2024-12-12T16:06:36Z |
publishDate | 2017-05-01 |
publisher | Elsevier |
record_format | Article |
series | Acta Pharmaceutica Sinica B |
spelling | doaj.art-ba3edd839311499e977dcdc7fbc8f9f92022-12-22T00:19:18ZengElsevierActa Pharmaceutica Sinica B2211-38352211-38432017-05-017339039410.1016/j.apsb.2016.12.008Structural analysis of recombinant human ubiquitin-conjugating enzyme UbcH5cFangshu WuJunsheng ZhuHonglin LiLili ZhuUbcH5c 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.http://www.sciencedirect.com/science/article/pii/S2211383516303677UbcH5cNF-κBUbiquitinationUbiquitin-conjugating enzymeCrystal structureInflammatory target |
spellingShingle | Fangshu Wu Junsheng Zhu Honglin Li Lili Zhu Structural analysis of recombinant human ubiquitin-conjugating enzyme UbcH5c Acta Pharmaceutica Sinica B UbcH5c NF-κB Ubiquitination Ubiquitin-conjugating enzyme Crystal structure Inflammatory target |
title | Structural analysis of recombinant human ubiquitin-conjugating enzyme UbcH5c |
title_full | Structural analysis of recombinant human ubiquitin-conjugating enzyme UbcH5c |
title_fullStr | Structural analysis of recombinant human ubiquitin-conjugating enzyme UbcH5c |
title_full_unstemmed | Structural analysis of recombinant human ubiquitin-conjugating enzyme UbcH5c |
title_short | Structural analysis of recombinant human ubiquitin-conjugating enzyme UbcH5c |
title_sort | structural analysis of recombinant human ubiquitin conjugating enzyme ubch5c |
topic | UbcH5c NF-κB Ubiquitination Ubiquitin-conjugating enzyme Crystal structure Inflammatory target |
url | http://www.sciencedirect.com/science/article/pii/S2211383516303677 |
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