Affordable Access

deepdyve-link
Publisher Website

The RING domain of TRIM69 promotes higher-order assembly.

Authors
  • Keown, Jeremy R1
  • Yang, Joy1
  • Black, Moyra M1
  • Goldstone, David C1
  • 1 School of Biological Sciences, University of Auckland, Private Bag 92019, Auckland, New Zealand. , (New Zealand)
Type
Published Article
Journal
Acta crystallographica. Section D, Structural biology
Publication Date
Oct 01, 2020
Volume
76
Issue
Pt 10
Pages
954–961
Identifiers
DOI: 10.1107/S2059798320010499
PMID: 33021497
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

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.

Report this publication

Statistics

Seen <100 times