Transcription factor interactions: basics on zippers

被引：126

作者：

Kerppola, Tom K. ^{[1
]}

Curran, Tom ^{[1
]}

机构：

[1] Roche Inst Mol Biol, Dept Mol Oncol & Virol, Nutley, NJ 07110 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1991年 / 1卷 / 01期

关键词：

D O I：

10.1016/0959-440X(91)90014-K

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 bZIP protein family of transcription factors has expanded dramatically and now includes several subfamilies that collectively define a consensus sequence; this includes the seven-residue repeat of leucines and a small number of shared residues in the basic region. The structure of the leucine zipper, a parallel coiled-coil that is stabilized by hydrophobic interactions, has been well established. The basic region assumes an alpha-helical conformation on binding DNA; however, the detailed structure of this region, as well as the mechanism of sequence recognition, remains unresolved.

引用

页码：71 / 79

页数：9

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