Retroviral restriction factor TRIM5alpha is a trimer |
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| Authors: | Mische Claudia C Javanbakht Hassan Song Byeongwoon Diaz-Griffero Felipe Stremlau Matthew Strack Bettina Si Zhihai Sodroski Joseph |
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| Affiliation: | Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Division of AIDS, Harvard Medical School, Boston, Massachusetts 02115, USA. |
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| 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. |
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