| Literature DB >> 16254380 |
Claudia C Mische1, Hassan Javanbakht, Byeongwoon Song, Felipe Diaz-Griffero, Matthew Stremlau, Bettina Strack, Zhihai Si, Joseph Sodroski.
Abstract
The retrovirus restriction factor TRIM5alpha targets the viral capsid soon after entry. Here we show that the TRIM5alpha protein oligomerizes into trimers. The TRIM5alpha coiled-coil and B30.2(SPRY) domains make important contributions to the formation and/or stability of the trimers. A functionally defective TRIM5alpha mutant with the RING and B-box 2 domains deleted can form heterotrimers with wild-type TRIM5alpha, accounting for the observed dominant-negative activity of the mutant protein. Trimerization potentially allows TRIM5alpha to interact with threefold pseudosymmetrical structures on retroviral capsids.Entities:
Mesh:
Substances:
Year: 2005 PMID: 16254380 PMCID: PMC1280198 DOI: 10.1128/JVI.79.22.14446-14450.2005
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103