CO-CRYSTAL STRUCTURE OF THE HNF-3/FORK HEAD DNA-RECOGNITION MOTIF RESEMBLES HISTONE-H5
CO-CRYSTAL STRUCTURE OF THE HNF-3/FORK HEAD DNA-RECOGNITION MOTIF RESEMBLES HISTONE-H5
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DOI：
10.1038/364412a0
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发表时间：
1993-07-29
期刊：
影响因子：
64.8
通讯作者：
BURLEY, SK
中科院分区：
文献类型：
--
作者：
CLARK, KL;HALAY, ED;BURLEY, SK
用2.5埃分辨率的X射线结晶学测定了与DNA络合的HNF-3/叉头DNA识别基序的三维结构。这种α/β蛋白通过与DNA骨架的相互作用，以及通过直接和水介导的主要和次要沟底接触，作为单体与B-DNA结合，导致13度弯曲。转录因子折叠与组蛋白H5的结构非常相似。在其氨基末端的一半，三个α-螺旋采用紧凑的结构，将第三个螺旋呈现给主槽。蛋白质的其余部分包括一个扭曲的、反平行的β结构和与小凹槽相互作用的随机卷曲。
The three-dimensional structure of an HNF-3/fork head DNA-recognition motif complexed with DNA has been determined by X-ray crystallography at 2.5 angstrom resolution. This alpha/beta protein binds B-DNA as a monomer, through interactions with the DNA backbone and through both direct and water-mediated major and minor groove base contacts, inducing a 13-degrees bend. The transcription factor fold is very similar to the structure of histone H5. In its amino-terminal half, three alpha-helices adopt a compact structure that presents the third helix to the major groove. The remainder of the protein includes a twisted, antiparallel beta-structure and random coil that interacts with the minor groove.