Solution structure of the DNA-binding domain of MafG

被引：41

作者：

Kusunoki, H

Motohashi, H

Katsuoka, F

Morohashi, A

Yamamoto, M

Tanaka, T ^{[1
]}

机构：

[1] Univ Tsukuba, Ctr Tsukuba Adv Res Alliance, Tsukuba, Ibaraki 3058577, Japan

[2] Univ Tsukuba, Inst Basic Med Sci, Tsukuba, Ibaraki 3058575, Japan

[3] Univ Tsukuba, Inst Appl Biochem, Tsukuba, Ibaraki 3058572, Japan

[4] Banyu Tsukuba Res Inst, Tsukuba, Ibaraki 3002611, Japan

来源：

NATURE STRUCTURAL BIOLOGY | 2002年 / 9卷 / 04期

基金：

日本学术振兴会;

关键词：

D O I：

10.1038/nsb771

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 Maf family proteins, which constitute a subgroup of basic region-leucine zipper (bZIP) proteins, function as transcriptional regulators of cellular differentiation. Together with the basic region, the Maf extended homology region (EHR), conserved only within the Maf family, defines the DNA binding specific to Mafs. Here we present the first NMR-derived structure of the DNA-binding domain (residues 1-76) of MafG, which contains the EHR and the basic region. The structure consists of three alpha-helices and resembles the fold of the DNA-binding domain of Skn-1, a developmental transcription factor of Caenorhabditis elegans. The structural similarity between MafG and Skn-1 enables us to propose a possible mechanism by which Maf family proteins recognize their consensus DNA sequences.

引用

页码：252 / 256

页数：5

共 31 条

[1] Twelve species of the nucleoid-associated protein from Escherichia coli -: Sequence recognition specificity and DNA binding affinity [J].