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

Autor:	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.; Department of Cardiovascular Sciences, Houston Methodist Research Institute, Houston, TX, USA., Zhang Z; Immunobiology and Transplant Science Center and Department of Surgery, Houston Methodist Research Institute, Houston, TX, USA.; Department of Surgery, Weill Cornell Medical College of Cornell University, New York, USA., Li XC; Immunobiology and Transplant Science Center and Department of Surgery, Houston Methodist Research Institute, Houston, TX, USA.; Department of Surgery, Weill Cornell Medical College of Cornell University, New York, USA.
Jazyk:	angličtina
Zdroj:	Computational and structural biotechnology journal [Comput Struct Biotechnol J] 2023 Apr 23; Vol. 21, pp. 2801-2808. Date of Electronic Publication: 2023 Apr 23 (Print Publication: 2023).
DOI:	10.1016/j.csbj.2023.04.022
Abstrakt:	Protein ubiquitination is a post-translation modification mediated by E3 ubiquitin ligases. The RING domain E3 ligases are the largest family of E3 ubiquitin ligases, they act as a scaffold, bringing the E2-ubiquitin complex and its substrate together to facilitate direct ubiquitin transfer. However, the quaternary structures of RING E3 ligases that perform ubiquitin transfer remain poorly understood. In this study, we solved the crystal structure of TRIM56, a member of the RING E3 ligase. The structure of the coiled-coil domain indicated that the two anti-parallel dimers bound together to form a tetramer at a small crossing angle. This tetramer structure allows two RING domains to exist on each side to form an active homodimer in supporting ubiquitin transfer from E2 to its nearby substrate recruited by the C-terminal domains on the same side. These findings suggest that the coiled-coil domain-mediated tetramer is a feasible scaffold for facilitating the recruitment and transfer of ubiquitin to accomplish E3 ligase activity. Competing Interests: None. (© 2023 The Authors.)
Databáze:	MEDLINE
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