A model of the full-length HIV-1 integrase dimer was constructed assembling the experimentally determined structures of the single domains. Subsequently, the three-domain protein-viral DNA complex was generated for the first time through an automated docking algorithm, obtained modifying the ESCHER program, a well-known method for protein-protein docking. A detailed study of the contacts established with DNA by the enzyme revealed that the predicted model reproduced the results of mutagenesis and cross-linking experiments, confirming the validity of our docking approach in predicting the base specificity in the DNA-protein interaction.
|Titolo:||Analysis of the full-length integrase DNA complex by a modified approach for DNA docking|
PEDRETTI, ALESSANDRO (Secondo)
|Parole Chiave:||HIV-1 integrase ; DNA–protein docking ; Full-length IN–DNA complex|
|Settore Scientifico Disciplinare:||Settore CHIM/08 - Chimica Farmaceutica|
|Data di pubblicazione:||31-ott-2003|
|Digital Object Identifier (DOI):||10.1016/j.bbrc.2003.09.120|
|Appare nelle tipologie:||01 - Articolo su periodico|