High-resolution view of HIV-1 reverse transcriptase initiation complexes and inhibition by NNRTI drugs

Initiation of HIV-1 reverse transcription occurs at the host tRNALys 3, which forms a complex with the 5’ end of the HIV-1 viral RNA and reverse transcriptase (RT). Here, the authors present the 2.8 Å cryo-EM structure of a minimal HIV-1 RT–vRNA–tRNALys 3 initiation complex (miniRTIC), and miniRTIC...

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Autores principales:	Betty Ha, Kevin P. Larsen, Jingji Zhang, Ziao Fu, Elizabeth Montabana, Lynnette N. Jackson, Dong-Hua Chen, Elisabetta Viani Puglisi
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/428ee5420f604c7da4a4e2a37fe10591
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spelling	oai:doaj.org-article:428ee5420f604c7da4a4e2a37fe105912021-12-02T15:38:20ZHigh-resolution view of HIV-1 reverse transcriptase initiation complexes and inhibition by NNRTI drugs10.1038/s41467-021-22628-92041-1723https://doaj.org/article/428ee5420f604c7da4a4e2a37fe105912021-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-22628-9https://doaj.org/toc/2041-1723Initiation of HIV-1 reverse transcription occurs at the host tRNALys 3, which forms a complex with the 5’ end of the HIV-1 viral RNA and reverse transcriptase (RT). Here, the authors present the 2.8 Å cryo-EM structure of a minimal HIV-1 RT–vRNA–tRNALys 3 initiation complex (miniRTIC), and miniRTIC structures with the bound non-nucleoside reverse transcriptase inhibitors nevirapine and efavirenz at 3.1 and 2.9 Å resolution, respectively.Betty HaKevin P. LarsenJingji ZhangZiao FuElizabeth MontabanaLynnette N. JacksonDong-Hua ChenElisabetta Viani PuglisiNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Betty Ha Kevin P. Larsen Jingji Zhang Ziao Fu Elizabeth Montabana Lynnette N. Jackson Dong-Hua Chen Elisabetta Viani Puglisi High-resolution view of HIV-1 reverse transcriptase initiation complexes and inhibition by NNRTI drugs
description	Initiation of HIV-1 reverse transcription occurs at the host tRNALys 3, which forms a complex with the 5’ end of the HIV-1 viral RNA and reverse transcriptase (RT). Here, the authors present the 2.8 Å cryo-EM structure of a minimal HIV-1 RT–vRNA–tRNALys 3 initiation complex (miniRTIC), and miniRTIC structures with the bound non-nucleoside reverse transcriptase inhibitors nevirapine and efavirenz at 3.1 and 2.9 Å resolution, respectively.
format	article
author	Betty Ha Kevin P. Larsen Jingji Zhang Ziao Fu Elizabeth Montabana Lynnette N. Jackson Dong-Hua Chen Elisabetta Viani Puglisi
author_facet	Betty Ha Kevin P. Larsen Jingji Zhang Ziao Fu Elizabeth Montabana Lynnette N. Jackson Dong-Hua Chen Elisabetta Viani Puglisi
author_sort	Betty Ha
title	High-resolution view of HIV-1 reverse transcriptase initiation complexes and inhibition by NNRTI drugs
title_short	High-resolution view of HIV-1 reverse transcriptase initiation complexes and inhibition by NNRTI drugs
title_full	High-resolution view of HIV-1 reverse transcriptase initiation complexes and inhibition by NNRTI drugs
title_fullStr	High-resolution view of HIV-1 reverse transcriptase initiation complexes and inhibition by NNRTI drugs
title_full_unstemmed	High-resolution view of HIV-1 reverse transcriptase initiation complexes and inhibition by NNRTI drugs
title_sort	high-resolution view of hiv-1 reverse transcriptase initiation complexes and inhibition by nnrti drugs
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/428ee5420f604c7da4a4e2a37fe10591
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High-resolution view of HIV-1 reverse transcriptase initiation complexes and inhibition by NNRTI drugs

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