Journal
VIROLOGY
Volume 353, Issue 1, Pages 234-246Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2006.05.017
Keywords
TRIM5 alpha; HIV-1; retroviral capsid; coiled-coil domain; trimerization
Categories
Funding
- NHLBI NIH HHS [HL54785] Funding Source: Medline
- NIAID NIH HHS [AI063987, AI45405, AI28691] Funding Source: Medline
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The coiled-coil domain of the tripartite motif (TRIM) family protein TRIM5 alpha is required for trimerization and function as an antiretroviral restriction factor. Unlike the coiled-coil regions of other related TRIM proteins, the coiled coil of TRIM5 alpha is not sufficient for multimerization. The linker region between the coiled-coil and B30.2 domains is necessary for efficient TRIM5 alpha trimerization. Most of the hydrophilic residues predicted to be located on the surface-exposed face of the coiled coil can be altered without compromising TRIM5 alpha antiviral activity against human immunodeficiency virus (HIV-1). However, changes that disrupt TRIM5 alpha trimerization proportionately affect the ability of TRIM5 alpha to bind HIV-1 capsid complexes. Therefore, TRIM5 alpha trimerization makes a major contribution to its avidity for the retroviral capsid, and to the ability to restrict virus infection. (c) 2006 Elsevier Inc. All rights reserved.
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