Unconventional plasticity of HIV-1 reverse transcriptase: how inhibitors could open a connection "gate" between allosteric and catalytic sites.
J Chem Inf Model
; 53(12): 3117-22, 2013 Dec 23.
Article
em En
| MEDLINE
| ID: mdl-24256065
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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Pirimidinas
/
Compostos de Vinila
/
HIV-1
/
Inibidores da Transcriptase Reversa
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Transcriptase Reversa do HIV
/
Simulação de Dinâmica Molecular
/
Simulação de Acoplamento Molecular
Limite:
Humans
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article