Targeted molecular dynamics (TMD) simulations allowed for identifying the chemical/structural features of the nucleotide-competitive HIV-1 inhibitor DAVP-1, which is responsible for the disruption of the T-shape motif between Try183 and Trp229 of the reverse transcriptase (RT). DAVP-1 promoted the opening of a connection “gate” between allosteric and catalytic sites of HIV-1 RT, thus explaining its peculiar mechanism of action and providing useful insights to develop novel nucleotide-competitive RT inhibitors.
Unconventional plasticity of hiv-1 reverse transcriptase: How inhibitors could open a connection "gate" between allosteric and catalytic sites / Luca, Bellucci; Lucilla, Angeli; Andrea, Tafi; Radi, Marco; Maurizio, Botta. - In: JOURNAL OF CHEMICAL INFORMATION AND MODELING. - ISSN 1549-9596. - 53:12(2013), pp. 3117-3122. [10.1021/ci400414s]
Unconventional plasticity of hiv-1 reverse transcriptase: How inhibitors could open a connection "gate" between allosteric and catalytic sites
RADI, Marco;
2013-01-01
Abstract
Targeted molecular dynamics (TMD) simulations allowed for identifying the chemical/structural features of the nucleotide-competitive HIV-1 inhibitor DAVP-1, which is responsible for the disruption of the T-shape motif between Try183 and Trp229 of the reverse transcriptase (RT). DAVP-1 promoted the opening of a connection “gate” between allosteric and catalytic sites of HIV-1 RT, thus explaining its peculiar mechanism of action and providing useful insights to develop novel nucleotide-competitive RT inhibitors.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
