Unconventional
Plasticity of HIV‑1 Reverse
Transcriptase: How Inhibitors Could Open a Connection “Gate”
between Allosteric and Catalytic Sites
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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