       Document 0371
 DOCN  M9630371
 TI    Interface peptides as structure-based human immunodeficiency virus
       reverse transcriptase inhibitors.
 DT    9603
 AU    Divita G; Baillon JG; Rittinger K; Chermann JC; Goody RS;
       Max-Planck-Institut fur Medizinische Forschung, Abteilung; Biophysik,
       Heidelberg, Germany.
 SO    J Biol Chem. 1995 Dec 1;270(48):28642-6. Unique Identifier : AIDSLINE
       MED/96081924
 AB    Reverse transcriptases from both human immunodeficiency viruses type 1
       and 2 are obligatory dimers. A tryptophan-rich repeat motif that is
       highly conserved between these proteins, as well as in the reverse
       transcriptase from simian immunodeficiency virus, has been postulated to
       be involved in hydrophobic subunit interactions. A synthetic 19-mer
       peptide covering part of this tryptophan repeat motif was recently shown
       to inhibit human immunodeficiency viruses type 1 reverse transcriptase
       subunit dimerization (Divita, G., Restle, T., Goody, R. S., Chermann,
       J.-C., and Baillon, J. G. (1994) J. Biol. Chem. 269, 13080-13083). In
       the present study, we show that the same peptide can also inhibit human
       immunodeficiency virus type 2 reverse transcriptase subunit
       dimerization, suggesting that the same inhibitors might be used as
       agents against both viruses as well as against variants of human
       immunodeficiency virus type 1 that differ from the variant against which
       they were developed. Under appropriate experimental conditions, e.g. at
       acidic pH, this peptide is also able to induce the dissociation of the
       enzyme from human immunodeficiency virus type 1.
 DE    Amino Acid Sequence  Biopolymers/CHEMISTRY  Enzyme Stability
       Hydrogen-Ion Concentration  HIV-1/*ENZYMOLOGY  HIV-2/*ENZYMOLOGY
       Molecular Sequence Data  Peptide Fragments/CHEMISTRY/*PHARMACOLOGY
       Reverse Transcriptase Inhibitors/CHEMISTRY/*PHARMACOLOGY  RNA-Directed
       DNA Polymerase/CHEMISTRY/*DRUG EFFECTS/METABOLISM  Support, Non-U.S.
       Gov't  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).

