Minor groove-binding architectural proteins: Structure, function, and DNA recognition

被引：219

作者：

Bewley, CA ^{[1
]}

Gronenborn, AM ^{[1
]}

Clore, GM ^{[1
]}

机构：

[1] NIDDKD, Chem Phys Lab, NIH, Bethesda, MD 20892 USA

来源：

ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE | 1998年 / 27卷

关键词：

TATA box binding protein; HMG-box proteins; integration host factor; HMG I(Y); DNA bending;

D O I：

10.1146/annurev.biophys.27.1.105

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：

To date, high-resolution structures have been solved for five different architectural proteins complexed to their DNA target sites. These include TATA-box-binding protein, integration host factor (IHF), high mobility group I(Y)[HMG I(Y)], and the HMG-box-containing proteins SRY and LEF-1. Each of these proteins interacts with DNA exclusively through minor groove contacts and alters DNA conformation. This paper reviews the structural features of these complexes and the roles they play in facilitating assembly of higher-order protein-DNA complexes and discusses elements that contribute to sequence-specific recognition and conformational changes.

引用

页码：105 / 131

页数：27

共 63 条

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