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Crystal structures of HIV-1 reverse transcriptase complexes with thiocarbamate non-nucleoside inhibitors

Journal Article · · Biochemical and Biophysical Research Communications
 [1]; ;  [1];  [2];  [3];  [4]
  1. Dipartimento di Scienze Farmaceutiche, Universita di Genova, viale Benedetto XV, 3, I-16132 Genova (Italy)
  2. Istituto Nazionale per la Ricerca sul Cancro (IST), Largo Rosanna Benzi, 10, I-16132 Genova (Italy)
  3. Department of Cell and Molecular Biology, Uppsala University, Biomedical Center, Box 596, SE-751 24 Uppsala (Sweden)
  4. Department of Biomolecular Sciences and Biotechnology, CNR-INFM, University of Milano, Via Celoria 26, I-20131 Milan (Italy)

O-Phthalimidoethyl-N-arylthiocarbamates (TCs) have been recently identified as a new class of potent HIV-1 reverse transcriptase (RT) non-nucleoside inhibitors (NNRTIs), by means of computer-aided drug design techniques [Ranise A. Spallarossa, S. Cesarini, F. Bondavalli, S. Schenone, O. Bruno, G. Menozzi, P. Fossa, L. Mosti, M. La Colla, et al., Structure-based design, parallel synthesis, structure-activity relationship, and molecular modeling studies of thiocarbamates, new potent non-nucleoside HIV-1 reverse transcriptase inhibitor isosteres of phenethylthiazolylthiourea derivatives, J. Med. Chem. 48 (2005) 3858-3873]. To elucidate the atomic details of RT/TC interaction and validate an earlier TC docking model, the structures of three RT/TC complexes were determined at 2.8-3.0 A resolution by X-ray crystallography. The conformations adopted by the enzyme-bound TCs were analyzed and compared with those of bioisosterically related NNRTIs.

OSTI ID:
21043590
Journal Information:
Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 4 Vol. 365; ISSN 0006-291X; ISSN BBRCA9
Country of Publication:
United States
Language:
English

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