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The RING domain of TRIM69 promotes higher‐order assembly
Author(s) -
Keown Jeremy R.,
Yang Joy,
Black Moyra M.,
Goldstone David C.
Publication year - 2020
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.374
H-Index - 138
ISSN - 2059-7983
DOI - 10.1107/s2059798320010499
Subject(s) - ring (chemistry) , vesicular stomatitis virus , trim , domain (mathematical analysis) , helix bundle , chemistry , helix (gastropod) , virus , microbiology and biotechnology , biology , crystallography , stereochemistry , biophysics , protein structure , virology , biochemistry , computer science , mathematics , mathematical analysis , ecology , organic chemistry , snail , operating system
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.