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J. Biol. Chem., Vol. 265, Issue 16, 8986-8988, Jun, 1990
Dimerization of human immunodeficiency virus type 1 reverse transcriptase. A target for chemotherapeutic intervention
T Restle, B Muller and RS Goody
Max-Planck-Institut fur Medizinische Forschung, Abteilung Biophysik, Heidelberg, Federal Republic of Germany.
Recombinant human immunodeficiency virus type 1 reverse transcriptase has
been used to investigate the process of dimer formation and the properties
of the different mono- and dimeric forms of the enzyme. The studies show
that reverse transcriptase activity is exclusively confined to the dimeric
forms. As we also demonstrate, the association rate constant between the
monomers is relatively low so that the dimer- monomer equilibrium is very
slowly established. This offers a new and potentially interesting target
for antiviral chemotherapy with presumably higher specificity than the
currently used nucleoside analogs (Yarchoan, R., Mitsuya, H., Myers, C.E.,
and Broder, S. (1989) N. Eng. J. Med. 321, 726-738), which in their active
triphosphorylated form are also inhibitors of cellular polymerases.

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Copyright © 1990 by the American Society for Biochemistry and Molecular Biology.
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