title: Structure-activity analyses of HIV-1 reverse transcriptase.
abstract: HIV-1 reverse transcriptase is a dimeric enzyme which can exist in both homodimeric (p66/p66) and heterodimeric (p66/p51) forms. The monomeric subunits are catalytically inert. However, during DNA synthesis by the dimeric enzyme, only one subunit (p66) appears to carry out the catalysis, while the second subunit serves only a supportive role. In the case of the p66/p66 homodimers, we find that both the subunits are catalytically competent as judged by the observation that a) primer binding occurs to both subunits and b) catalytically inert dimers can be partially activated by replacement of one of the two inactive p66 subunits.
authors.affiliation: Department of Biochemistry & Molecular Biology UMDNJ, New Jersey Medical School, Newark 07103.
authors.forename: A
authors.initials: A
authors.lastname: Basu
authors.forename: S
authors.initials: S
authors.lastname: Basu
authors.forename: M J
authors.initials: MJ
authors.lastname: Modak
mesh_terms: D000163:Acquired Immunodeficiency Syndrome / Q000378:metabolism*; D004789:Enzyme Activation; D015497:HIV-1 / Q000201:enzymology*; D046911:Macromolecular Substances; D012194:RNA-Directed DNA Polymerase / Q000737:chemistry / Q000378:metabolism*
chemical_list: D046911:Macromolecular Substances; D012194:RNA-Directed DNA Polymerase