Evolution of inhibitor-resistant natural mutant forms of HIV-1 protease probed by pre-steady state kinetic analysis

Pre-steady state kinetic analysis of mechanistic features of substrate binding and processing is crucial for insight into the evolution of inhibitor-resistant forms of HIV-1 protease. These data may provide a correct vector for rational drug design assuming possible intrinsic dynamic effects. These...

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Veröffentlicht in:	Biochimie 2017-11, Vol.142, p.125-134
Hauptverfasser:	Zakharova, Maria Yu, Kuznetsova, Alexandra A., Kaliberda, Elena N., Dronina, Maria A., Kolesnikov, Alexander V., Kozyr, Arina V., Smirnov, Ivan V., Rumsh, Lev D., Fedorova, Olga S., Knorre, Dmitry G., Gabibov, Alexander G., Kuznetsov, Nikita A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Active site evolution Amino Acid Sequence Drug Resistance, Viral Enzyme-substrate interaction FRET HIV Protease - genetics HIV Protease - metabolism HIV-1 - enzymology HIV-1 - genetics HIV-1 protease Kinetics Mechanism of protease action Models, Molecular Multidrug-resistant mutant Mutation Pre-steady state kinetics Protease Inhibitors - pharmacology Protein Conformation Stopped-flow analysis
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