@article{f112d14ff0f74574b07d4b699a5b5260,
title = "Ile178 of HIV-1 reverse transcriptase is critical for inhibiting the viral integrase",
abstract = "HIV-1 reverse transcriptase (RT) was shown to inhibit in vitro the viral integrase (IN). We have reported previously that an RT-derived 20-residue peptide binds IN and inhibits its enzymatic activities. In this peptide, Leu168, Phe171, Gln174, and Ile178 were predicted to be involved in IN inhibition. In the presented study, these residues were mutagenized and the resulting peptides were tested for binding and inhibiting IN activities. Ile178 was found to be the major contributor to IN inhibition, probably by interacting with IN residue Gly149. As Gly149 is a key IN residue, this inhibition probably results from a steric hindrance of the IN active site.",
keywords = "HIV-1, Inhibition, Integrase, Mutation, Peptides, Reverse transcriptase",
author = "{Oz Gleenberg}, Iris and Yehuda Goldgur and Amnon Hizi",
note = "Funding Information: Peptide 4286 was a generous gift obtained from the NIH AIDS Research and Reference Reagent Program, Division of AIDS, NIAID, NIH. We thank the Israeli Science Foundation (Grant No. 405/02) for support.",
year = "2007",
month = dec,
day = "7",
doi = "10.1016/j.bbrc.2007.09.086",
language = "אנגלית",
volume = "364",
pages = "48--52",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Elsevier B.V.",
number = "1",
}