HIV-2 protease is inactivated after oxidation at the dimer interface and activity can be partly restored with methionine sulphoxide reductase

Biochemical Journal

Volumn 346, Issue 2, 2000, Pages 305-311

  Davis, David A ^a   Newcomb, Fonda M ^a   Moskovitz, Jackob ^b   Wingfield, Paul T ^c   Stahl, Stephen J ^c   Kaufman, Joshua ^c   Fales, Henry M ^b   Levine, Rodney L ^b   Yarchoan, Robert ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

^c NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES   (United States)

Author keywords

Polyprotein processing; Redox regulation; Retroviruses; Thioredoxin; Viral maturation

Indexed keywords

DIMER; HYDROGEN PEROXIDE; METHIONINE SULFOXIDE; OXIDOREDUCTASE; PAPAIN; PROTEINASE;

AMINO ACID SEQUENCE; ARTICLE; ENZYME ACTIVITY; ENZYME METABOLISM; HUMAN IMMUNODEFICIENCY VIRUS 2; MASS SPECTROMETRY; NONHUMAN; OXIDATION; PEPTIDE MAPPING; PRIORITY JOURNAL; PROTEIN PROCESSING; VIRUS INACTIVATION;

AMINO ACID SEQUENCE; ASPARTIC ENDOPEPTIDASES; DIMERIZATION; ENZYME ACTIVATION; HIV-2; HUMANS; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; OXIDOREDUCTASES; SEQUENCE ALIGNMENT; VIRUS REPLICATION;

HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1; HUMAN IMMUNODEFICIENCY VIRUS 2; RNA VIRUSES;

EID: 0034163437     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3460305     Document Type: Article

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