Meinke G, Sigler P B
Department of Molecular Biophysics and Biochemistry and the Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06511, USA.
Nat Struct Biol. 1999 May;6(5):471-7. doi: 10.1038/8276.
The 2.7 A X-ray crystal structure of the DNA-binding domain (DBD) of the orphan nuclear receptor, nerve growth factor-induced-B (NGFI-B), complexed to its high-affinity DNA target, represents the first structure analysis of a nuclear receptor DBD bound as a monomer to DNA. The structure of the core DBD and its interactions with the major groove of the DNA are similar to previously crystallographically solved DBD-DNA complexes in this superfamily; however, residues C-terminal to this core form a separate and unique substructure that interacts extensively and in a sequence-specific way with the minor groove of its DNA target, in particular with the characteristic 3 A-T base-pair identity element that extends 5' to the usual nuclear receptor half-site (AGGTCA).
孤儿核受体神经生长因子诱导蛋白B(NGFI-B)的DNA结合结构域(DBD)与其高亲和力DNA靶标形成复合物的2.7埃X射线晶体结构,代表了核受体DBD以单体形式与DNA结合的首次结构分析。核心DBD的结构及其与DNA大沟的相互作用与该超家族中先前通过晶体学解析的DBD-DNA复合物相似;然而,该核心C端的残基形成了一个单独且独特的亚结构,该亚结构与其DNA靶标的小沟广泛且以序列特异性方式相互作用,特别是与特征性的3个A-T碱基对识别元件相互作用,该元件在通常的核受体半位点(AGGTCA)的5'端延伸。