Electrostatics Plays a Crucial Role in HIV-1 Protease Substrate Binding, Drugs Fail to Take Advantage
Author:
Affiliation:
1. Department of Biotechnology and BJM School of Biosciences, Indian Institute of Technology Madras, Chennai 600036, India
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.0c00341
Reference49 articles.
1. WHO fact sheets. HIV/AIDS. https://www.who.int/news-room/fact-sheets/detail/hiv-aids (accessed 2020-02-19).
2. Recent Progress in the Development of HIV-1 Protease Inhibitors for the Treatment of HIV/AIDS
3. Solution NMR Evidence That the HIV-1 Protease Catalytic Aspartyl Groups Have Different Ionization States in the Complex Formed with the Asymmetric Drug KNI-272
4. Structure of HIV-1 protease in complex with potent inhibitor KNI-272 determined by high-resolution X-ray and neutron crystallography
5. Ionization state of the catalytic dyad Asp25/25′ in the HIV-1 protease: NMR studies of site-specifically 13C labelled HIV-1 protease prepared by total chemical synthesis
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