THE CRYSTAL-STRUCTURE OF THE ESTROGEN-RECEPTOR DNA-BINDING DOMAIN BOUND TO DNA - HOW RECEPTORS DISCRIMINATE BETWEEN THEIR RESPONSE ELEMENTS
THE CRYSTAL-STRUCTURE OF THE ESTROGEN-RECEPTOR DNA-BINDING DOMAIN BOUND TO DNA - HOW RECEPTORS DISCRIMINATE BETWEEN THEIR RESPONSE ELEMENTS
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DOI：
10.1016/0092-8674(93)90390-c
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发表时间：
1993-11-05
期刊：
影响因子：
64.5
通讯作者：
RHODES, D
中科院分区：
文献类型：
--
作者：
SCHWABE, JWR;CHAPMAN, L;RHODES, D
核激素受体是配体激活的DNA结合转录因子的超家族。我们已经确定了雌激素受体DNA结合域和DNA之间完全特异性复合物的晶体结构（在2.4埃）。该蛋白结合作为一个对称的二聚体的回文结合位点组成的两个6 bp的共识半位点与三个插入碱基对。这种结构揭示了蛋白质如何识别自己的半位点序列，而不是相关糖皮质激素受体的半位点序列，后者仅相差两个碱基对。由于所有核激素受体都识别这两个共有半位点序列中的一个或另一个，因此这种识别机制通常适用于整个受体家族。
The nuclear hormone receptors are a superfamily of ligand-activated DNA-binding transcription factors. We have determined the crystal structure (at 2.4 angstrom) of the fully specific complex between the DNA-binding domain from the estrogen receptor and DNA. The protein binds as a symmetrical dimer to its palindromic binding site consisting of two 6 bp consensus half sites with three intervening base pairs. This structure reveals how the protein recognizes its own half site sequence rather than that of the related glucocorticoid receptor, which differs by only two base pairs. Since all nuclear hormone receptors recognize one or the other of these two consensus half site sequences, this recognition mechanism applies generally to the whole receptor family.