Seeing the sites: Unlike classical nonnucleoslde 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. (Nucleoside analogue RT inhibitor (NRTI) binding site Is shown in red.) (Figure Presented) © 2010 Wiley-VCH Verlag GmbH & Co. KCaA.
Freisz, S., Bec, G., Radi, M., Wolff, P., Crespan, E., Angeli, L., et al. (2010). Crystal Structure of HIV-1 Reverse Transcriptase Bound to a Non-Nucleoside Inhibitor with a Novel Mechanism of Action. ANGEWANDTE CHEMIE. INTERNATIONAL EDITION, 49(10), 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;Angeli, Lucilla;Botta, Maurizio;
2010-01-01
Abstract
Seeing the sites: Unlike classical nonnucleoslde 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. (Nucleoside analogue RT inhibitor (NRTI) binding site Is shown in red.) (Figure Presented) © 2010 Wiley-VCH Verlag GmbH & Co. KCaA.
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https://hdl.handle.net/11365/9355
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