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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adaptor Proteins, Signal Transducing*
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Amino Acid Sequence
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Binding Sites
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DNA Nucleotidyltransferases / chemistry*
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DNA Nucleotidyltransferases / genetics
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DNA Nucleotidyltransferases / metabolism
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DNA-Binding Proteins / chemistry*
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DNA-Binding Proteins / genetics
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Escherichia coli / genetics
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GRB2 Adaptor Protein
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HIV-1 / enzymology*
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Integrases
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Magnetic Resonance Spectroscopy
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Models, Molecular
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Molecular Sequence Data
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Peptide Fragments / chemistry*
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Peptide Fragments / genetics
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Protein Conformation
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Proteins / chemistry
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Recombinant Proteins / chemistry
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Sequence Homology
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Solutions
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Spectrin / chemistry
Substances
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Adaptor Proteins, Signal Transducing
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DNA-Binding Proteins
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GRB2 Adaptor Protein
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Peptide Fragments
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Proteins
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Recombinant Proteins
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Solutions
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Spectrin
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DNA Nucleotidyltransferases
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Integrases