Dynamic conformational changes in the rhesus TRIM5α dimer dictate the potency of HIV-1 restriction

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• 作者：Rajan Lamichhane^a ; Santanu Mukherjee^b ; Nikolai Smolin^c ; Raymond F. Pauszek III^a ; Margret Bradley^b ; Jaya Sastri^d ; Seth L. Robia^c ; David Millar^a ; Edward M. Campbell^b ;
• 关键词：Single molecule FRET ; TRIM5alpha ; HIV-1 ; Molecular dynamics simulation ; smFRET ; Restriction factor ; Coiled coil ; Dimer ; Tripartite Motif
• 刊名：Virology
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：500
• 期：Complete
• 页码：161-168
• 全文大小：1123 K
• 卷排序：500

文摘

Conformational dynamics of the rhesus macaque TRIM5α dimer were monitored by single molecule FRET. Three distinct conformations of the dimer were observed. Mutations which increase or decrease HIV-1 restriction shift correlate with altered occupancy of distinct FRET states. Conformational changes observed may facilitate binding or abortive disassembly of the HIV-1 capsid by rhTRIM5α.