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Title: Molecular basis for substrate recognition and drug resistance from 1.1 to 1.6 Å resolution crystal structures of HIV-1 protease mutants with substrate analogs

Journal Article · · FEBS J.
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  1. GSU
+ Show Author Affiliations

Research Organization:
Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Organization:
OTHER U.S. STATESNIHOTHER
OSTI ID:
1170422
Journal Information:
FEBS J., Vol. 272, Issue (20) ; 10, 2005
Country of Publication:
United States
Language:
ENGLISH

References (40)

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Substrate Shape Determines Specificity of Recognition for HIV-1 Protease journal March 2002
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Crystallographic Analysis of Human Immunodeficiency Virus 1 Protease with an Analog of the Conserved CA-p2 Substrate. Interactions with Frequently Occurring Glutamic Acid Residue at P2' Position of Substrates journal October 1997
Structural implications of drug-resistant mutants of HIV-1 protease: High-resolution crystal structures of the mutant protease/substrate analogue complexes journal January 2001
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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 † journal January 1996
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Improved methods for building protein models in electron density maps and the location of errors in these models journal March 1991
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures journal October 1991

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