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Retroviral Restriction Factor TRIM5α Is a Trimer.

Authors :
Claudia C. Mische
Hassan Javanbakht
Byeongwoon Song
Felipe Diaz-Griffero
Matthew Stremlau
Bettina Strack
Zhihai Si
Joseph Sodroski
Source :
Journal of Virology. Nov2005, Vol. 79 Issue 22, p14446-14450. 5p. 4 Graphs.
Publication Year :
2005

Abstract

The retrovirus restriction factor TRIM5α 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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
0022538X
Volume :
79
Issue :
22
Database :
Academic Search Index
Journal :
Journal of Virology
Publication Type :
Academic Journal
Accession number :
19332610
Full Text :
https://doi.org/10.1128/JVI.79.22.14446-14450.2005