Different Enzyme Conformations Induce Different Mechanistic Traits in HIV‐1 Protease

Author:

Coimbra João T. S.1ORCID,Neves Rui P. P.1ORCID,Cunha Ana V.23,Ramos Maria J.1ORCID,Fernandes Pedro A.1ORCID

Affiliation:

1. LAQV/REQUIMTE Departamento de Química e Bioquímica Faculdade de Ciências Universidade do Porto Rua do Campo Alegre, s/n 4169-007 Porto Portugal

2. Scientific Computing Group Oak Ridge National Laboratory 1 Bethel Valley Rd 37831-6373 Oak Ridge TN USA

3. Presnt address: Department of Chemistry University of Antwerp Groenenborgerlaan 171 2020 Antwerp Belgium

Funder

Ministério da Ciência, Tecnologia e Ensino Superior

Fundação para a Ciência e a Tecnologia

Oak Ridge National Laboratory

U.S. Department of Energy

Publisher

Wiley

Subject

General Chemistry,Catalysis,Organic Chemistry

Reference49 articles.

1. World Health Organization Geneva (Switzerland) can be found underhttps://www.who.int/news-room/fact-sheets/detail/hiv-aids 2019(accessed July 2021).

2. HIV Drug Resistance Report 2019 World Health Organization Geneva (Switzerland)2019(WHO/CDS/HIV/19.21).

3. Exploration of the effects of sequence variations between HIV-1 and HIV-2 proteases on their three-dimensional structures

4. Picomolar to Micromolar: Elucidating the Role of Distal Mutations in HIV-1 Protease in Conferring Drug Resistance

5. Visualizing Tetrahedral Oxyanion Bound in HIV-1 Protease Using Neutrons: Implications for the Catalytic Mechanism and Drug Design

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