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The RING domain of TRIM69 promotes higher-order assembly
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Keown, Jeremy R., Yang, Joy, Black, Moyra M. and Goldstone, David C. (2020) The RING domain of TRIM69 promotes higher-order assembly. Acta Crystallographica Section D Structural Biology, 76 (10). pp. 954-961. doi:10.1107/S2059798320010499 ISSN 2059-7983.
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Official URL: http://doi.org/10.1107/S2059798320010499
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.
Item Type: | Journal Article | ||||
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||
Journal or Publication Title: | Acta Crystallographica Section D Structural Biology | ||||
Publisher: | International Union of Crystallography | ||||
ISSN: | 2059-7983 | ||||
Official Date: | 1 October 2020 | ||||
Dates: |
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Volume: | 76 | ||||
Number: | 10 | ||||
Page Range: | pp. 954-961 | ||||
DOI: | 10.1107/S2059798320010499 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Open Access (Creative Commons) |
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