Cryo-EM structure of human MG53 homodimer-Reference-Cited by-同舟云学术

Cryo-EM structure of human MG53 homodimer

Published:2022-09-16 Issue:17 Volume:479 Page:1909-1916
ISSN:0264-6021
Container-title:Biochemical Journal
language:en
Short-container-title:

Author:

Niu Yange¹²,Chen Gengjia¹²,Lv Fengxiang¹,Xiao Rui-Ping¹³,Hu Xinli¹,Chen Lei¹²³^ORCID

Affiliation:

1. 1State Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking University, Beijing 100871, China

2. 2National Biomedical Imaging Center, Peking University, Beijing 100871, China

3. 3Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, China

Abstract

MG53 is a tripartite motif (TRIM) family E3 ligase and plays important biological functions. Here we present the cryo-EM structure of human MG53, showing that MG53 is a homodimer consisting of a ‘body’ and two ‘wings’. Intermolecular interactions are mainly distributed in the ‘body’ which is relatively stable, while two ‘wings’ are more dynamic. The overall architecture of MG53 is distinct from those of TRIM20 and TRIM25, illustrating the broad structural diversity of this protein family.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

https://portlandpress.com/biochemj/article-pdf/479/17/1909/944268/bcj-2022-0385.pdf

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