Structural highlights
Publication Abstract from PubMed
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.
Analysis of the full-length integrase-DNA complex by a modified approach for DNA docking.,De Luca L, Pedretti A, Vistoli G, Barreca ML, Villa L, Monforte P, Chimirri A Biochem Biophys Res Commun. 2003 Oct 31;310(4):1083-8. PMID:14559226[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ De Luca L, Pedretti A, Vistoli G, Barreca ML, Villa L, Monforte P, Chimirri A. Analysis of the full-length integrase-DNA complex by a modified approach for DNA docking. Biochem Biophys Res Commun. 2003 Oct 31;310(4):1083-8. PMID:14559226
