Retroviral restriction factor TRIM5α is a trimer

Claudia C. Mische, Hassan Javanbakht, Byeongwoon Song, Felipe Diaz-Griffero, Matthew Stremlau, Bettina Strack, Zhihai Si, Joseph Sodroski

Research output: Contribution to journalArticlepeer-review

110 Scopus citations


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 languageEnglish (US)
Pages (from-to)14446-14450
Number of pages5
JournalJournal of virology
Issue number22
StatePublished - Nov 2005
Externally publishedYes

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology


Dive into the research topics of 'Retroviral restriction factor TRIM5α is a trimer'. Together they form a unique fingerprint.

Cite this