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- W1993021726 abstract "The tripartite motif (TRIM) protein, TRIM5α, restricts some retroviruses, including human immunodeficiency virus (HIV-1), from infecting the cells of particular species. TRIM proteins contain RING, B-box, coiled-coil and, in some cases, B30.2(SPRY) domains. We investigated the properties of human TRIM family members closely related to TRIM5. These TRIM proteins, like TRIM5α, assembled into homotrimers and co-localized in the cytoplasm with TRIM5α. TRIM5α turned over more rapidly than related TRIM proteins. TRIM5α, TRIM34 and TRIM6 associated with HIV-1 capsid–nucleocapsid complexes assembled in vitro ; the TRIM5α and TRIM34 interactions with these complexes were dependent on their B30.2(SPRY) domains. Only TRIM5α potently restricted infection by the retroviruses studied; overexpression of TRIM34 resulted in modest inhibition of simian immunodeficiency virus (SIV mac ) infection. In contrast to the other TRIM genes examined, TRIM5 exhibited evidence of positive selection. The unique features of TRIM5α among its TRIM relatives underscore its special status as an antiviral factor." @default.
- W1993021726 created "2016-06-24" @default.
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- W1993021726 date "2007-04-01" @default.
- W1993021726 modified "2023-09-30" @default.
- W1993021726 title "Unique features of TRIM5α among closely related human TRIM family members" @default.
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- W1993021726 doi "https://doi.org/10.1016/j.virol.2006.10.035" @default.
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