期刊
JOURNAL OF VIROLOGY
卷 79, 期 22, 页码 14446-14450出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.79.22.14446-14450.2005
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资金
- NHLBI NIH HHS [P50 HL054785, HL54785] Funding Source: Medline
- NIAID NIH HHS [R01 AI063987, AI063987, P30 AI028691, AI28691] Funding Source: Medline
The retrovirus restriction factor TRIM5 alpha targets the viral capsid soon after entry. Here we show that the TRIM5 alpha protein oligomerizes into trimers. The TRIM5 alpha coiled-coil and B30.2(SPRY) domains make important contributions to the formation and/or stability of the trimers. A functionally defective TRIM5a mutant with the RING and B-box 2 domains deleted can form heterotrimers with wild-type TRIM5 alpha, accounting for the observed dominant-negative activity of the mutant protein. Trimerization potentially allows TRIM5 alpha to interact with threefold pseudosymmetrical structures on retroviral capsids.
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