Retroviral restriction factor TRIM5alpha is a trimer.

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.

journal_name

J Virol

journal_title

Journal of virology

authors

Mische CC,Javanbakht H,Song B,Diaz-Griffero F,Stremlau M,Strack B,Si Z,Sodroski J

doi

10.1128/JVI.79.22.14446-14450.2005

subject

Has Abstract

pub_date

2005-11-01 00:00:00

pages

14446-50

issue

22

eissn

0022-538X

issn

1098-5514

pii

79/22/14446

journal_volume

79

pub_type

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