CRYSTALLOGRAPHIC ANALYSIS OF THE INTERACTION OF THE GLUCOCORTICOID RECEPTOR WITH DNA
CRYSTALLOGRAPHIC ANALYSIS OF THE INTERACTION OF THE GLUCOCORTICOID RECEPTOR WITH DNA
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DOI：
10.1038/352497a0
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发表时间：
1991-08-08
期刊：
影响因子：
64.8
通讯作者：
SIGLER, PB
中科院分区：
文献类型：
--
作者：
LUISI, BF;XU, WX;SIGLER, PB
本文报道糖皮质激素受体DNA结合区与DNA复合的两种晶体结构。该结构域有一个球状折叠，其中包含两个不同的构象和功能的锌成核的亚结构。当它结合DNA时，结构域二聚化，将亚基置于相邻的大沟中。在一个复合体中，DNA具有对称的共有靶序列;在第二个复合体中，靶的半位点之间的中心间隔大一个碱基对。这导致一个亚基与共有靶半位点特异性相互作用，而另一个亚基与非同源元件非特异性相互作用。DNA诱导的二聚体固定了亚基识别表面的分离，使得半位点之间的间隔成为靶序列身份的关键特征。
Two crystal structures of the glucocorticoid receptor DNA-binding domain complexed with DNA are reported. The domain has a globular fold which contains two Zn-nucleated substructures of distinct conformation and function. When it binds DNA, the domain dimerizes, placing the subunits in adjacent major grooves. In one complex, the DNA has the symmetrical consensus target sequence; in the second, the central spacing between the target's half-sites is larger by one base pair. This results in one subunit interacting specifically with the consensus target half-site and the other nonspecifically with a noncognate element. The DNA-induced dimer fixes the separation of the subunits' recognition surfaces so that the spacing between the half-sites becomes a critical feature of the target sequence's identity.