Max通过二聚体b/HLH/Z结构域识别其同源DNA。

Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain.

作者信息

Ferré-D'Amaré A R, Prendergast G C, Ziff E B, Burley S K

机构信息

Laboratories of Molecular Biophysics, Rockefeller University, New York, New York 10021.

出版信息

Nature. 1993 May 6;363(6424):38-45. doi: 10.1038/363038a0.

DOI:10.1038/363038a0

PMID:8479534

Abstract

The three-dimensional structure of the basic/helix-loop-helix/leucine zipper domain of the transcription factor Max complexed with DNA has been determined by X-ray crystallography at 2.9 A resolution. Max binds as a dimer to its recognition sequence CACGTG by direct contacts between the alpha-helical basic region and the major groove. This symmetric homodimer, a new protein fold, is a parallel, left-handed, four-helix bundle, with each monomer containing two alpha-helical segments separated by a loop. The two alpha-helical segments are composed of the basic region plus helix 1 and helix 2 plus the leucine repeat, respectively. As in GCN4, the leucine repeat forms a parallel coiled coil.

摘要

转录因子Max与DNA复合的碱性/螺旋-环-螺旋/亮氨酸拉链结构域的三维结构已通过X射线晶体学在2.9埃分辨率下确定。Max以二聚体形式通过α-螺旋碱性区域与大沟之间的直接接触结合到其识别序列CACGTG上。这种对称的同型二聚体是一种新的蛋白质折叠形式，是一个平行的、左手的四螺旋束，每个单体包含由一个环隔开的两个α-螺旋段。这两个α-螺旋段分别由碱性区域加螺旋1和螺旋2加亮氨酸重复序列组成。与GCN4一样，亮氨酸重复序列形成一个平行的卷曲螺旋。