小沟结合型结构蛋白：结构、功能及DNA识别
Minor groove-binding architectural proteins: structure, function, and DNA recognition.
作者信息
Bewley C A, Gronenborn A M, Clore G M
机构信息
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-520, USA.
出版信息
Annu Rev Biophys Biomol Struct. 1998;27:105-31. doi: 10.1146/annurev.biophys.27.1.105.
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.
迄今为止，已经解析出了五种不同的结构蛋白与其DNA靶位点复合物的高分辨率结构。这些蛋白包括TATA盒结合蛋白、整合宿主因子（IHF）、高迁移率族蛋白I（Y）[HMG I（Y）]，以及含有HMG盒的蛋白SRY和LEF-1。这些蛋白中的每一种都仅通过小沟接触与DNA相互作用，并改变DNA构象。本文综述了这些复合物的结构特征及其在促进高阶蛋白质-DNA复合物组装中所起的作用，并讨论了有助于序列特异性识别和构象变化的因素。
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