ZINC FINGER DNA RECOGNITION - CRYSTAL-STRUCTURE OF A ZIF268-DNA COMPLEX AT 2.1-A
ZINC FINGER DNA RECOGNITION - CRYSTAL-STRUCTURE OF A ZIF268-DNA COMPLEX AT 2.1-A
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DOI：
10.1126/science.2028256
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发表时间：
1991-05-10
期刊：
影响因子：
56.9
通讯作者：
PABO, CO
中科院分区：
文献类型：
--
作者：
PAVLETICH, NP;PABO, CO
锌指DNA结合基序存在于许多调节真核基因表达的蛋白质中。含有来自Zif 268（小鼠立即早期蛋白质）的三个锌指和一个共有DNA结合位点的复合物的晶体结构已被确定为2.1埃分辨率，并精确到18.2%的晶体学R因子。在这种复合物中，锌指结合在B-DNA的大沟中，并部分缠绕在双螺旋周围。每个手指都与DNA有相似的关系，并在三个碱基对的亚位点上进行主要接触。来自α-螺旋氨基末端部分的残基接触碱基，并且大多数接触是与DNA的富含鸟嘌呤的链进行的。这种结构为理解锌指如何识别DNA提供了一个框架，并表明这种基序可能为设计新的DNA结合蛋白提供有用的基础。
The zinc finger DNA-binding motif occurs in many proteins that regulate eukaryotic gene expression. The crystal structure of a complex containing the three zinc fingers from Zif268 (a mouse immediate early protein) and a consensus DNA-binding site has been determined at 2.1 angstroms resolution and refined to a crystallographic R factor of 18.2 percent. In this complex, the zinc fingers bind in the major groove of B-DNA and wrap partway around the double helix. Each finger has a similar relation to the DNA and makes its primary contacts in a three-base pair subsite. Residues from the amino-terminal portion of an alpha-helix contact the bases, and most of the contacts are made with the guanine-rich strand of the DNA. This structure provides a framework for understanding how zinc fingers recognize DNA and suggests that this motif may provide a useful basis for the design of novel DNA-binding proteins.