1IHV
SOLUTION STRUCTURE OF THE DNA BINDING DOMAIN OF HIV-1 INTEGRASE, NMR, MINIMIZED AVERAGE STRUCTURE
Summary for 1IHV
| Entry DOI | 10.2210/pdb1ihv/pdb |
| Descriptor | HIV-1 INTEGRASE (1 entity in total) |
| Functional Keywords | dna-binding protein, aids, polyprotein, dna binding protein |
| Biological source | Human immunodeficiency virus 1 |
| Total number of polymer chains | 2 |
| Total formula weight | 12278.37 |
| Authors | Clore, G.M.,Lodi, P.J.,Ernst, J.A.,Gronenborn, A.M. (deposition date: 1995-05-12, release date: 1996-10-14, Last modification date: 2024-05-22) |
| Primary citation | Lodi, P.J.,Ernst, J.A.,Kuszewski, J.,Hickman, A.B.,Engelman, A.,Craigie, R.,Clore, G.M.,Gronenborn, A.M. Solution structure of the DNA binding domain of HIV-1 integrase. Biochemistry, 34:9826-9833, 1995 Cited by PubMed 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. PubMed: 7632683DOI: 10.1021/bi00031a002 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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