Lodi P J, Ernst J A, Kuszewski J, Hickman A B, Engelman A, Craigie R, Clore G M, Gronenborn A M
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA.
Biochemistry. 1995 Aug 8;34(31):9826-33. doi: 10.1021/bi00031a002.
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.
通过多维核磁共振光谱法确定了HIV-1整合酶DNA结合结构域（第220 - 270位氨基酸残基）的溶液结构。该蛋白在溶液中为二聚体，每个亚基由一个五链β桶组成，其拓扑结构与SH3结构域非常相似。二聚体由包含第2、3和4链的堆叠β界面形成，两个三链反平行β折叠片分别来自每个亚基，彼此反平行排列。二聚体的一个表面由β1链和β2链之间的环界定，形成一个鞍形凹槽，其横截面尺寸约为24×23×12埃。根据突变数据显示，参与DNA结合的赖氨酸264从该表面突出，这表明鞍形凹槽是潜在的DNA结合位点。
