Retroviral restriction factor TRIM5alpha is a trimer.
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.
Mische
Claudia C
CC
Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Division of AIDS, Harvard Medical School, Boston, Massachusetts 02115, USA.
Javanbakht
Hassan
H
Song
Byeongwoon
B
Diaz-Griffero
Felipe
F
Stremlau
Matthew
M
Strack
Bettina
B
Si
Zhihai
Z
Sodroski
Joseph
J
D000818:Animals; D001665:Binding Sites; D002213:Capsid / Q000378:metabolism; D036022:Capsid Proteins / Q000378:metabolism*; D002460:Cell Line; D002522:Chlorocebus aethiops; D014644:Genetic Variation; D006367:HeLa Cells; D006801:Humans; D008253:Macaca mulatta; D011506:Proteins / Q000378:metabolism*; D012190:Retroviridae / Q000378:metabolism*; D014162:Transfection; D044767:Ubiquitin-Protein Ligases
D036022:Capsid Proteins; D011506:Proteins; C482587:TRIM5(alpha) protein, rhesus monkey; D044767:Ubiquitin-Protein Ligases