Retroviral restriction factor TRIM5α is a trimer

被引：109

作者：

Mische, CC

Javanbakht, H

Song, BW

Diaz-Griffero, F

Stremnlau, M

Strack, B

Si, ZH

Sodroski, J

机构：

[1] Harvard Univ, Dept Canc Immunol & AIDS, Div Aids, Dana Farber Canc Inst,Sch Med, Boston, MA 02115 USA

[2] Harvard Univ, Sch Publ Hlth, Dept Immunol & Infect Dis, Boston, MA 02115 USA

来源：

JOURNAL OF VIROLOGY | 2005年 / 79卷 / 22期

关键词：

D O I：

10.1128/JVI.79.22.14446-14450.2005

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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.

引用

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页码：14446 / 14450

页数：5

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