Terminal interface conformations modulate dimer stability prior to amino terminal autoprocessing of HIV-1 protease

Biochemistry

Volumn 51, Issue 5, 2012, Pages 1041-1050

  Agniswamy, Johnson ^a   Sayer, Jane M ^b   Weber, Irene T ^a   Louis, John M ^b  

^a GEORGIA STATE UNIVERSITY   (United States)

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

Author keywords

[No Author keywords available]

Indexed keywords

AUTOPROCESSING; DIMER DISSOCIATION; DIMER FORMATION; DIMER INTERFACE; DIMERIC STRUCTURE; DISSOCIATION CONSTANT; HIGH RESOLUTION CRYSTAL STRUCTURE; HIV-1 PROTEASE; INFECTIOUS VIRUS; INTERFACE RESIDUES; N-TERMINALS; PEPTIDE BONDS; REVERSE TRANSCRIPTASES; SAQUINAVIR;

DISEASES; DISSOCIATION; HYDROGEN BONDS; QUANTUM OPTICS; VIRUSES;

DIMERS;

DARUNAVIR; DIMER; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE; SAQUINAVIR;

AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CARBOXY TERMINAL SEQUENCE; CONFORMATION; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DIMERIZATION; DISSOCIATION CONSTANT; HYDROGEN BOND; PRIORITY JOURNAL; TEMPERATURE MEASUREMENT; THERMOSTABILITY;

AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; GAG GENE PRODUCTS, HUMAN IMMUNODEFICIENCY VIRUS; HIV PROTEASE; HYDROLYSIS; MOLECULAR SEQUENCE DATA; POL GENE PRODUCTS, HUMAN IMMUNODEFICIENCY VIRUS; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; PROTEIN PRECURSORS; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STABILITY; THERMODYNAMICS;

HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 84856710288     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201809s     Document Type: Article

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