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<jats:p>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.</jats:p>

Original publication

DOI

10.1107/s2059798320010499

Type

Journal article

Journal

Acta Crystallographica Section D Structural Biology

Publisher

International Union of Crystallography (IUCr)

Publication Date

01/10/2020

Volume

76

Pages

954 - 961