Structural highlights
Function
[TRI69_HUMAN] May have E3 ubiquitin-protein ligase activity. May play a role in apoptosis.[1]
Publication Abstract from PubMed
Members of the TRIM protein family have been shown to inhibit a range of viral infections. Recently, TRIM69 was identified as a potent inhibitor of Vesicular stomatitis Indiana virus infection, with its inhibition being dependent upon multimerization. Using SEC-MALLS analysis, it is demonstrated that the assembly of TRIM69 is mediated through the RING domain and not the Bbox domain as has been shown for other TRIM proteins. Using X-ray crystallography, the structure of the TRIM69 RING domain has been determined to a resolution of 2.1 A, the oligomerization interface has been identified and regions outside the four-helix bundle have been observed to form interactions that are likely to support assembly.
The RING domain of TRIM69 promotes higher-order assembly.,Keown JR, Yang J, Black MM, Goldstone DC Acta Crystallogr D Struct Biol. 2020 Oct 1;76(Pt 10):954-961. doi:, 10.1107/S2059798320010499. Epub 2020 Sep 16. PMID:33021497[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Han Y, Li R, Gao J, Miao S, Wang L. Characterisation of human RING finger protein TRIM69, a novel testis E3 ubiquitin ligase and its subcellular localisation. Biochem Biophys Res Commun. 2012 Dec 7;429(1-2):6-11. doi:, 10.1016/j.bbrc.2012.10.109. Epub 2012 Nov 3. PMID:23131556 doi:http://dx.doi.org/10.1016/j.bbrc.2012.10.109
- ↑ Keown JR, Yang J, Black MM, Goldstone DC. The RING domain of TRIM69 promotes higher-order assembly. Acta Crystallogr D Struct Biol. 2020 Oct 1;76(Pt 10):954-961. doi:, 10.1107/S2059798320010499. Epub 2020 Sep 16. PMID:33021497 doi:http://dx.doi.org/10.1107/S2059798320010499