Solution Structure of the DNA Binding Domain of HIV-1 Integrase
Copyright policy )Solution Structure of the DNA Binding Domain of HIV-1 Integrase
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.
- National Institutes of Health United States
- National Institute of Health Pakistan
- National Institute of Diabetes and Digestive and Kidney Diseases United States
Models, Molecular, Binding Sites, Magnetic Resonance Spectroscopy, Integrases, Protein Conformation, Molecular Sequence Data, Proteins, Sequence Homology, Spectrin, Peptide Fragments, Recombinant Proteins, DNA-Binding Proteins, Solutions, DNA Nucleotidyltransferases, Escherichia coli, HIV-1, Amino Acid Sequence, Adaptor Proteins, Signal Transducing, GRB2 Adaptor Protein
Models, Molecular, Binding Sites, Magnetic Resonance Spectroscopy, Integrases, Protein Conformation, Molecular Sequence Data, Proteins, Sequence Homology, Spectrin, Peptide Fragments, Recombinant Proteins, DNA-Binding Proteins, Solutions, DNA Nucleotidyltransferases, Escherichia coli, HIV-1, Amino Acid Sequence, Adaptor Proteins, Signal Transducing, GRB2 Adaptor Protein
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