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Cryo-EM structure of human MG53 homodimer.
Niu, Yange; Chen, Gengjia; Lv, Fengxiang; Xiao, Rui-Ping; Hu, Xinli; Chen, Lei.
  • Niu Y; State 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.
  • Chen G; National Biomedical Imaging Center, Peking University, Beijing 100871, China.
  • Lv F; State 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.
  • Xiao RP; National Biomedical Imaging Center, Peking University, Beijing 100871, China.
  • Hu X; State 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.
  • Chen L; State 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.
Biochem J ; 479(17): 1909-1916, 2022 09 16.
Article en En | MEDLINE | ID: mdl-36053137
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.
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Proteínas Portadoras / Proteínas de Motivos Tripartitos / Proteínas de la Membrana Límite: Humans Idioma: En Año: 2022 Tipo del documento: Article
Texto completo
Imprimir
XML
PubMed Links
Search on Google

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Proteínas Portadoras / Proteínas de Motivos Tripartitos / Proteínas de la Membrana Límite: Humans Idioma: En Año: 2022 Tipo del documento: Article