The L76V drug resistance mutation decreases the dimer stability and rate of autoprocessing of HIV-1 protease by reducing internal hydrophobic contacts

Biochemistry

Volumn 50, Issue 21, 2011, Pages 4786-4795

  Louis, John M ^a   Zhang, Ying ^b   Sayer, Jane M ^a   Wang, Yuan Fang ^b   Harrison, Robert W ^b   Weber, Irene T ^b  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^b GEORGIA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AUTOPROCESSING; DIMER DISSOCIATION; DRUG RESISTANCE; HIV-1 PROTEASE; HYDROPHOBIC CONTACT; HYDROPHOBIC INTERACTIONS; ISOTHERMAL TITRATION CALORIMETRY; LIGAND DISSOCIATION; MAIN CHAINS; MOLECULAR MECHANISM; N-TERMINALS; POLAR INTERACTIONS; SAQUINAVIR;

COMPLEXATION; DIFFERENTIAL SCANNING CALORIMETRY; DIMERS; DISSOCIATION; HYDROGEN; HYDROGEN BONDS; UREA;

HYDROPHOBICITY;

ASPARTIC ACID; DARUNAVIR; DIMER; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE; ISOLEUCINE; LOPINAVIR; LYSINE; SAQUINAVIR; THREONINE; UREA; VALINE;

ARTICLE; CHEMICAL INTERACTION; CRYSTAL STRUCTURE; DENATURATION; DIFFERENTIAL SCANNING CALORIMETRY; DISSOCIATION CONSTANT; HUMAN IMMUNODEFICIENCY VIRUS 1; HYDROGEN BOND; HYDROPHOBICITY; ISOTHERMAL TITRATION CALORIMETRY; PRIORITY JOURNAL; PROTEIN PROCESSING; PROTEIN STABILITY; VIRUS MUTATION; VIRUS RESISTANCE;

CALORIMETRY; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; DRUG RESISTANCE, VIRAL; HIV PROTEASE; MODELS, MOLECULAR; MUTATION; PROTEIN CONFORMATION; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;

HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 79958096391     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200033z     Document Type: Article

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