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• W2011068404 abstract "The coiled-coil domain of the tripartite motif (TRIM) family protein TRIM5α 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 TRIM5α is not sufficient for multimerization. The linker region between the coiled-coil and B30.2 domains is necessary for efficient TRIM5α trimerization. Most of the hydrophilic residues predicted to be located on the surface-exposed face of the coiled coil can be altered without compromising TRIM5α antiviral activity against human immunodeficiency virus (HIV-1). However, changes that disrupt TRIM5α trimerization proportionately affect the ability of TRIM5α to bind HIV-1 capsid complexes. Therefore, TRIM5α trimerization makes a major contribution to its avidity for the retroviral capsid, and to the ability to restrict virus infection." @default.
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• W2011068404 date "2006-09-01" @default.
• W2011068404 modified "2023-10-14" @default.
• W2011068404 title "Characterization of TRIM5α trimerization and its contribution to human immunodeficiency virus capsid binding" @default.
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• W2011068404 doi "https://doi.org/10.1016/j.virol.2006.05.017" @default.
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