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THE DNA-BINDING DOMAIN OF HIV-1 INTEGRASE HAS AN SH3-LIKE FOLD

被引：209
作者：
EIJKELENBOOM, APAM
LUTZKE, RAP
BOELENS, R
PLASTERK, RHA
KAPTEIN, R
HARD, K
机构：
[1] UNIV UTRECHT,BIJVOET CTR BIOMOLEC RES,3584 CH UTRECHT,NETHERLANDS
[2] NETHERLANDS CANC INST,DIV MOLEC BIOL,1066 CX AMSTERDAM,NETHERLANDS
来源：
NATURE STRUCTURAL BIOLOGY | 1995年 / 2卷 / 09期
关键词：
D O I：
10.1038/nsb0995-807
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：
We have determined the solution structure of the DNA-binding domain of HIV-1 integrase by nuclear magnetic resonance spectroscopy. In solution, this carboxy-terminal region of integrase forms a homodimer, consisting of two structures that closely resemble Src-homology 3 (SH3) domains. Lys 264 previously identified by mutagenesis studies to be important for DNA binding of the integrase, as well as several adjacent basic amino acids are solvent exposed, The identification of an SH3-like domain in integrase provides a new potential target for drug design.
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页码：807 / 810
页数：4
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