title: Solution structure of the DNA binding domain of HIV-1 integrase.
abstract: The solution structure of the DNA binding domain of HIV-1 integrase (residues 220-270) has been determined by multidimensional NMR spectroscopy. The protein is a dimer in solution, and each subunit is composed of a five-stranded beta-barrel with a topology very similar to that of the SH3 domain. The dimer is formed by a stacked beta-interface comprising strands 2, 3, and 4, with the two triple-stranded antiparallel beta-sheets, one from each subunit, oriented antiparallel to each other. One surface of the dimer, bounded by the loop between strands beta 1 and beta 2, forms a saddle-shaped groove with dimensions of approximately 24 x 23 x 12 A in cross section. Lys264, which has been shown from mutational data to be involved in DNA binding, protrudes from this surface, implicating the saddle-shaped groove as the potential DNA binding site.
authors.affiliation: Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA.
authors.forename: P J
authors.initials: PJ
authors.lastname: Lodi
authors.forename: J A
authors.initials: JA
authors.lastname: Ernst
authors.forename: J
authors.initials: J
authors.lastname: Kuszewski
authors.forename: A B
authors.initials: AB
authors.lastname: Hickman
authors.forename: A
authors.initials: A
authors.lastname: Engelman
authors.forename: R
authors.initials: R
authors.lastname: Craigie
authors.forename: G M
authors.initials: GM
authors.lastname: Clore
authors.forename: A M
authors.initials: AM
authors.lastname: Gronenborn
mesh_terms: D048868:Adaptor Proteins, Signal Transducing; D000595:Amino Acid Sequence; D001665:Binding Sites; D004254:DNA Nucleotidyltransferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D051380:GRB2 Adaptor Protein; D015497:HIV-1 / Q000201:enzymology*; D019426:Integrases; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry; D017385:Sequence Homology; D012996:Solutions; D013049:Spectrin / Q000737:chemistry
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D004268:DNA-Binding Proteins; D051380:GRB2 Adaptor Protein; D010446:Peptide Fragments; D011506:Proteins; D011994:Recombinant Proteins; D012996:Solutions; D013049:Spectrin; D004254:DNA Nucleotidyltransferases; D019426:Integrases