Dynamics of “Flap” Structures in Three HIV-1 Protease/Inhibitor Complexes Probed by Total Chemical Synthesis and Pulse-EPR Spectroscopy-Reference-Cited by-同舟云学术

Dynamics of “Flap” Structures in Three HIV-1 Protease/Inhibitor Complexes Probed by Total Chemical Synthesis and Pulse-EPR Spectroscopy

Published:2008-12-31 Issue:3 Volume:131 Page:884-885
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Torbeev Vladimir Yu.¹,Raghuraman H.¹,Mandal Kalyaneswar¹,Senapati Sanjib¹,Perozo Eduardo¹,Kent Stephen B. H.¹

Affiliation:

1. Institute for Biophysical Dynamics, Departments of Chemistry and of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois 60637, and Department of Biotechnology,, Indian Institute of Technology Madras, Chennai 600036, India

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja806526z

Reference13 articles.

1. Targeting structural flexibility in HIV-1 protease inhibitor binding

2. Flap opening and dimer-interface flexibility in the free and inhibitor-bound HIV protease, and their implications for function

3. Binding Pathways of Ligands to HIV-1 Protease: Coarse-grained and Atomistic Simulations

4. Catalytic contribution of flap-substrate hydrogen bonds in "HIV-1 protease" explored by chemical synthesis.

5. Interflap Distances in HIV-1 Protease Determined by Pulsed EPR Measurements

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