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.


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 Å, 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.

Keywords: RING domains; TRIM proteins; TRIM69; tripartite motif.

MeSH terms

  • Amino Acid Motifs
  • Humans
  • Models, Molecular*
  • Protein Domains*
  • Protein Multimerization*
  • Tripartite Motif Proteins / chemistry*
  • Ubiquitin-Protein Ligases / chemistry*


  • Tripartite Motif Proteins
  • TRIM69 protein, human
  • Ubiquitin-Protein Ligases