Enzymatic and structural analysis of the I47A mutation contributing to the reduced susceptibility to HIV protease inhibitor lopinavir

Lopinavir (LPV) is a second‐generation HIV protease inhibitor (PI) designed to overcome resistance development in patients undergoing long‐term antiviral therapy. The mutation of isoleucine at position 47 of the HIV protease (PR) to alanine is associated with a high level of resistance to LPV. In th...

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Veröffentlicht in:	Protein science 2008-09, Vol.17 (9), p.1555-1564
Hauptverfasser:	Šašková, Klára Grantz, Kožíšek, Milan, Lepšík, Martin, Brynda, Jiří, Řezáčová, Pavlína, Václavíková, Jana, Kagan, Ron M., Machala, Ladislav, Konvalinka, Jan
Format:	Artikel
Sprache:	eng
Schlagworte:	Alanine - metabolism Amino Acid Substitution antiviral resistance development Catalysis Computational Biology Disease Susceptibility Drug Resistance, Viral - genetics enzyme kinetics Escherichia coli - genetics HIV Protease - chemistry HIV Protease - genetics HIV Protease - isolation & purification HIV Protease - metabolism HIV protease inhibitors HIV Protease Inhibitors - chemistry HIV Protease Inhibitors - metabolism HIV Protease Inhibitors - pharmacology Human immunodeficiency virus Humans Hydrogen Bonding Hydrogen-Ion Concentration Kinetics Lopinavir Models, Molecular molecular recognition Protein Structure, Secondary Pyrimidinones - chemistry Pyrimidinones - metabolism Pyrimidinones - pharmacology Recombinant Proteins - antagonists & inhibitors Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification X‐ray structure
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