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Article

HIV-1 protease dimer interface mutations that compensate for viral reverse transcriptase instability in infectious virions.

Journal of molecular biology - 14 Sept 2007

Olivares Isabel, Mulky Alok, Boross Peter I, Tözsér József, Kappes John C, López-Galíndez Cecilio, Menéndez-Arias Luis

Abstract excerpt

Mature enzymes encoded within the human immunodeficiency virus type 1 (HIV-1) genome (protease (PR), reverse transcriptase (RT) and integrase (IN)) derive from proteolytic processing of a large polyprotein (Gag-Pol). Gag-Pol processing is catalyzed by the viral PR, which is active as a homodimer. The HIV-1 RT functions as a heterodimer (p66/p51) composed of subunits of 560 and 440 amino acid residues,...

Topics

Animals
Cell Line
Dimerization
Enzyme Stability
HIV Protease
HIV Reverse Transcriptase
HIV-1
Humans
Mutation
Urea
Virion

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Virus Replication

Source

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Identifiers

PMID: 17651754
DOI: 10.1016/j.jmb.2007.06.073
PMCID: PMC2696282

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