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Article

Conformational asymmetry of human immunodeficiency virus-1 protease flaps increases along the darunavir drug resistance pathway.

Protein science : a publication of the Protein Society - 1 Sept 2026

Guerrero Michel, Zadorozhnyi Roman, Lin Guowu, Quinn Caitlin M, Calero Guillermo, Kurt-Yilmaz Nese, Schiffer Celia A, Polenova Tatyana, Gronenborn Angela M, Ishima Rieko

Abstract excerpt

Under selective drug pressure, the structure and dynamics of HIV-1 protease (PR) evolve to confer resistance to the drug. Here, we report on the conformational changes in PR flaps for drug-resistance mutations using 19F nuclear magnetic resonance (NMR) spectroscopy. We prepared wild-type (wt) PR and its three mutant variants containing 4, 10, or 11 mutations, namely 4Mut, 10Mut, and 11Mut, that were previously...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 42554278
DOI: 10.1002/pro.70736
PMCID: PMC13439748

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

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