Data di Pubblicazione:
2005
Citazione:
Molecular dynamics studies of the full-length integrase-DNA complex / L. De Luca, G. Vistoli, A. Pedretti, M.L. Barreca, A. Chimirri. - In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. - ISSN 0006-291X. - 336:4(2005), pp. 1010-1016.
Abstract:
We have carried out a molecular dynamics (MD) simulation of full-length HIV-1 integrase (IN) dimer complexed with viral DNA with the aim of gaining information about the enzyme motion and investigating the movement of the catalytic flexible loop (residues 140-149) thought to be essential in the catalytic mechanism of IN. During the simulation, we observed quite a different behavior of this region in the presence or absence of the viral DNA. In particular, the MD results underline the crucial role of the residue Tyr143 in the mechanism of integration of viral DNA into the host chromosome. The present findings confirm the experimental data (e.g., site-directed mutagenesis experiments) showing that the loop is involved in the integration reactions and its mobility is correlated with the catalytic, activity of HIV-1 integrase.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
1WKN; Dynamics simulation; Full-length IN-DNA complex; HIV-1 integrase
Elenco autori:
L. De Luca, G. Vistoli, A. Pedretti, M.L. Barreca, A. Chimirri
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