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Reversible Oxidative Modification as a Mechanism for Regulating Retroviral Protease Dimerization and Activation

By David A. Davis, Cara A. Brown, Fonda M. Newcomb, Emily S. Boja, Henry M. Fales, Joshua Kaufman, Stephen J. Stahl, Paul Wingfield and Robert Yarchoan

Abstract

Human immunodeficiency virus protease activity can be regulated by reversible oxidation of a sulfur-containing amino acid at the dimer interface. We show here that oxidation of this amino acid in human immunodeficiency virus type 1 protease prevents dimer formation. Moreover, we show that human T-cell leukemia virus type 1 protease can be similarly regulated through reversible glutathionylation of its two conserved cysteine residues. Based on the known three-dimensional structures and multiple sequence alignments of retroviral proteases, it is predicted that the majority of retroviral proteases have sulfur-containing amino acids at the dimer interface. The regulation of protease activity by the modification of a sulfur-containing amino acid at the dimer interface may be a conserved mechanism among the majority of retroviruses

Topics: Structure and Assembly
Publisher: American Society for Microbiology
Year: 2003
DOI identifier: 10.1128/JVI.77.5.3319-3325.2003
OAI identifier: oai:pubmedcentral.nih.gov:149757
Provided by: PubMed Central
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