The retrovirus restriction factor TRIM5αa targets the viral capsid soon after entry. Here we show that the TRIM5α protein oligomerizes into trimers. The TRIM5α coiled-coil and B30.2(SPRY) domains make important contributions to the formation and/or stability of the trimers. A functionally defective TRIM5α mutant with the RING and B-box 2 domains deleted can form heterotrimers with wild-type TRIM5α, accounting for the observed dominant-negative activity of the mutant protein. Trimerization potentially allows TRIM5α to interact with threefold pseudosymmetrical structures on retroviral capsids.
|Original language||English (US)|
|Number of pages||5|
|Journal||Journal of virology|
|Publication status||Published - Nov 1 2005|
ASJC Scopus subject areas
- Insect Science