| Literature DB >> 7632683 |
P J Lodi1, J A Ernst, J Kuszewski, A B Hickman, A Engelman, R Craigie, G M Clore, A M Gronenborn.
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.Entities:
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Year: 1995 PMID： 7632683 DOI： 10.1021/bi00031a002
Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162