A 2.2 angstrom resolution crystal structure of a designed zinc finger protein bound to DNA
A 2.2 angstrom resolution crystal structure of a designed zinc finger protein bound to DNA
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DOI：
10.1038/nsb1196-940
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发表时间：
1996-11-01
期刊：
影响因子：
--
通讯作者：
Berg, JM
中科院分区：
文献类型：
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作者：
Kim, CA;Berg, JM
近年来，基于Cys（2）His（2）锌指结构域串联阵列的序列特异性DNA结合蛋白的设计和筛选已成为研究热点。虽然这些设计蛋白的DNA结合特性已被广泛研究，但位点特异性结合的结构基础尚未得到实验验证。在这里，我们报告的晶体结构的蛋白质之间的复合物由三个共识序列为基础的锌指结构域和一个寡核苷酸对应于一个有利的DNA结合位点。这种结构揭示了相对简单的模块化相互作用和结构适应，以补偿接触残基侧链长度的差异。
Considerable recent effort has been devoted to the design and selection of sequence-specific DNA binding proteins based on tandem arrays of Cys(2)His(2) zinc finger domains, While the DNA binding properties of these designed proteins have been studied extensively, the structural basis for site-specific binding has not been examined experimentally. Here we report the crystal structure of a complex between a protein comprised of three consensus-sequence-based zinc finger domains and an oligonucleotide corresponding to a favourable DNA binding site. This structure reveals relatively simple modular interactions and structural adaptations that compensate for differences in contact residue side-chain lengths.