Unlike classical non-nucleoside HIV-1 reverse transcriptase (RT) inhibitors (NNRTI; active site in blue), DAVP-1 is a non-nucleoside RT inhibitor that competes with the nucleotide substrate (NcRTI). The X-ray structure of DAVP-1 bound to the unligated RT shows a new inhibitor binding site close to the polymerase active site.
Crystal Structure of HIV-1 Reverse Transcriptase Bound to a Non-Nucleoside Inhibitor with a Novel Mechanism of Action / Séverine, Freisz; Guillaume, Bec; Radi, Marco; Philippe, Wolff; Emmanuele, Crespan; Lucilla, Angeli; Philippe, Dumas; Giovanni, Maga; Maurizio, Botta; Eric, Ennifar. - In: ANGEWANDTE CHEMIE. INTERNATIONAL EDITION. - ISSN 1433-7851. - 49:(2010), pp. 1805-1808. [10.1002/anie.200905651]
Crystal Structure of HIV-1 Reverse Transcriptase Bound to a Non-Nucleoside Inhibitor with a Novel Mechanism of Action
RADI, Marco;
2010-01-01
Abstract
Unlike classical non-nucleoside HIV-1 reverse transcriptase (RT) inhibitors (NNRTI; active site in blue), DAVP-1 is a non-nucleoside RT inhibitor that competes with the nucleotide substrate (NcRTI). The X-ray structure of DAVP-1 bound to the unligated RT shows a new inhibitor binding site close to the polymerase active site.| File | Dimensione | Formato | |
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