Abstract
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) |
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Pages (from-to) | 14446-14450 |
Number of pages | 5 |
Journal | Journal of virology |
Volume | 79 |
Issue number | 22 |
DOIs | |
State | Published - Nov 2005 |
Externally published | Yes |
ASJC Scopus subject areas
- Microbiology
- Immunology
- Insect Science
- Virology