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Article

Transient HIV-1 Gag-protease interactions revealed by paramagnetic NMR suggest origins of compensatory drug resistance mutations.

Proceedings of the National Academy of Sciences of the United States of America - 1 Nov 2016

Deshmukh Lalit, Louis John M, Ghirlando Rodolfo, Clore G Marius

Abstract excerpt

Cleavage of the group-specific antigen (Gag) polyprotein by HIV-1 protease represents the critical first step in the conversion of immature noninfectious viral particles to mature infectious virions. Selective pressure exerted by HIV-1 protease inhibitors, a mainstay of current anti-HIV-1 therapies, results in the accumulation of drug resistance mutations in both protease and Gag. Surprisingly, a large number of...

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Share to Drug Resistance, Viral

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to gag Gene Products, Human Immunodeficiency Virus

Share to HIV Protease

Share to HIV Protease Inhibitors

Share to Magnetic Resonance Spectroscopy

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Share to Protein Structure, Secondary

Source

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Identifiers

PMID: 27791180
DOI: 10.1073/pnas.1615342113
PMCID: PMC5098610

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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