Disulfide reduction in CD4 domain 1 or 2 Is essential for interaction with HIV glycoprotein 120 (gp120), which impairs thioredoxin-driven CD4 dimerization

Journal of Biological Chemistry

Volumn 289, Issue 15, 2014, Pages 10455-10465

  Cerutti, Nichole ^a   Killick, Mark ^a   Jugnarain, Vinesh ^a   Papathanasopoulos, Maria ^a   Capovilla, Alexio ^a  

^a UNIVERSITY OF THE WITWATERSRAND MEDICAL SCHOOL   (South Africa)

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; DIMERIZATION; DIMERS; GLYCOPROTEINS; ISOMERIZATION; ISOMERS; RECOMBINANT PROTEINS; REDOX REACTIONS; SULFUR COMPOUNDS; VIRUSES;

ANTIGEN PRESENTATION; DISULFIDE REDUCTION; EXCHANGE REACTION; HUMAN IMMUNODEFICIENCY VIRUS; MEMBRANE-BOUND; OXIDO-REDUCTASES; PATHOGENIC EFFECTS; PROTEIN DISULFIDE ISOMERASES;

T-CELLS;

ALANINE; CD4 ANTIGEN; CYSTEINE; DIMER; DISULFIDE; GLYCOPROTEIN GP 120; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; OXIDOREDUCTASE; PROTEIN DISULFIDE ISOMERASE; T LYMPHOCYTE RECEPTOR; THIOREDOXIN; THIOREDOXIN REDUCTASE;

ANTIGEN FUNCTION; ANTIGEN PRESENTATION; ARTICLE; CATALYSIS; CELL SURFACE; COMPLEX FORMATION; CONTROLLED STUDY; DIMERIZATION; DISULFIDE BOND; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS; ISOMER; ISOMERIZATION; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; VIRUS ENTRY;

CD4; DISULFIDE; GP120; HIV; REDOX; THIOL; THIOREDOXIN;

ANTIGEN PRESENTATION; ANTIGENS, CD4; CELL MEMBRANE; DIMERIZATION; DISULFIDES; ENZYME-LINKED IMMUNOSORBENT ASSAY; HEK293 CELLS; HIV ENVELOPE PROTEIN GP120; HIV-1; HUMANS; KINETICS; OXIDATION-REDUCTION; OXIDOREDUCTASES; OXYGEN; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; THERMODYNAMICS; THIOREDOXINS;

EID: 84898623415     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.539353     Document Type: Article

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