TRIM56 coiled-coil domain structure provides insights into its E3 ligase functions.

Lou, Xiaohua; Ma, Binbin; Zhuang, Yuan; Xiao, Xiang; Minze, Laurie J; Xing, Junji; Zhang, Zhiqiang; Li, Xian C

Lou, Xiaohua; Ma, Binbin; Zhuang, Yuan; Xiao, Xiang; Minze, Laurie J; Xing, Junji; Zhang, Zhiqiang; Li, Xian C.

Afiliação

Lou X; Immunobiology and Transplant Science Center and Department of Surgery, Houston Methodist Research Institute, Houston, TX, USA.
Ma B; Immunobiology and Transplant Science Center and Department of Surgery, Houston Methodist Research Institute, Houston, TX, USA.
Zhuang Y; Immunobiology and Transplant Science Center and Department of Surgery, Houston Methodist Research Institute, Houston, TX, USA.
Xiao X; Immunobiology and Transplant Science Center and Department of Surgery, Houston Methodist Research Institute, Houston, TX, USA.
Minze LJ; Immunobiology and Transplant Science Center and Department of Surgery, Houston Methodist Research Institute, Houston, TX, USA.
Xing J; Immunobiology and Transplant Science Center and Department of Surgery, Houston Methodist Research Institute, Houston, TX, USA.
Zhang Z; Department of Cardiovascular Sciences, Houston Methodist Research Institute, Houston, TX, USA.
Li XC; Immunobiology and Transplant Science Center and Department of Surgery, Houston Methodist Research Institute, Houston, TX, USA.

Comput Struct Biotechnol J ; 21: 2801-2808, 2023.

Article em En | MEDLINE | ID: mdl-37168870

Palavras-chave

Coiled-coil domain; Crystal structure; E3 Ubiquitin ligase; Hydrophobic interactions; TRIM56; Tetramerization

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: Comput Struct Biotechnol J Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Estados Unidos País de publicação: Holanda

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