SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF HIV-1 INTEGRASE

被引：259

作者：

LODI, PJ

ERNST, JA

KUSZEWSKI, J

HICKMAN, AB

ENGELMAN, A

CRAIGIE, R

CLORE, GM

GRONENBORN, AM

机构：

[1] NIDDKD,CHEM PHYS LAB,BETHESDA,MD 20892

[2] NIDDKD,MOLEC BIOL LAB,BETHESDA,MD 20892

来源：

BIOCHEMISTRY | 1995年 / 34卷 / 31期

关键词：

D O I：

10.1021/bi00031a002

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 Angstrom 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.

引用

页码：9826 / 9833

页数：8

共 48 条

[1] SOLUTION STRUCTURE AND DNA-BINDING PROPERTIES OF A THERMOSTABLE PROTEIN FROM THE ARCHAEON SULFOLOBUS-SOLFATARICUS [J].