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

Protein Science

Volumn 17, Issue 9, 2008, Pages 1555-1564

  Šašková, Klára Grantz ^a,b   Kožíšek, Milan ^a,b   Lepšík, Martin ^a   Brynda, Jiří ^a,c   Řezáčová, Pavlína ^a,c   Václavíková, Jana ^a   Kagan, Ron M ^d   Machala, Ladislav ^e   Konvalinka, Jan ^a,b,c  

^a INSTITUTE OF ORGANIC CHEMISTRY AND BIOCHEMISTRY   (Czech Republic)

^b CHARLES UNIVERSITY   (Czech Republic)

^c INSTITUTE OF MOLECULAR GENETICS   (Czech Republic)

^d QUEST DIAGNOSTICS NICHOLS INSTITUTE   (United States)

^e UNIVERSITY HOSPITAL BULOVKA   (Czech Republic)

Author keywords

Antiviral resistance development; Enzyme kinetics; HIV protease inhibitors; Molecular recognition; X ray structure

Indexed keywords

AMPRENAVIR; ATAZANAVIR; BRECANAVIR; INDINAVIR; ISOLEUCINE; LOPINAVIR; PROTEINASE; RITONAVIR; SAQUINAVIR;

AIDS PATIENT; AMINO ACID SUBSTITUTION; ARTICLE; CRYSTAL STRUCTURE; ENZYME ANALYSIS; ENZYME STRUCTURE; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN INTERACTION; WILD TYPE;

ALANINE; AMINO ACID SUBSTITUTION; CATALYSIS; COMPUTATIONAL BIOLOGY; DISEASE SUSCEPTIBILITY; DRUG RESISTANCE, VIRAL; ESCHERICHIA COLI; HIV PROTEASE; HIV PROTEASE INHIBITORS; HUMANS; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; PROTEIN STRUCTURE, SECONDARY; PYRIMIDINONES; RECOMBINANT PROTEINS;

EID: 50049088535     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.036079.108     Document Type: Article

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