Kim C A, Berg J M
Department of Chemistry, Johns Hopkins University, Baltimore, Maryland 21218, USA.
Nat Struct Biol. 1996 Nov;3(11):940-5. doi: 10.1038/nsb1196-940.
Considerable recent effort has been devoted to the design and selection of sequence-specific DNA binding proteins based on tandem arrays of Cys2His2 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.
最近，人们投入了大量精力，基于Cys2His2锌指结构域的串联阵列来设计和选择序列特异性DNA结合蛋白。虽然这些设计蛋白的DNA结合特性已得到广泛研究，但位点特异性结合的结构基础尚未经过实验检验。在此，我们报道了一种由三个基于共有序列的锌指结构域组成的蛋白与一个对应于有利DNA结合位点的寡核苷酸之间的复合物的晶体结构。该结构揭示了相对简单的模块化相互作用和结构适应性，以补偿接触残基侧链长度的差异。
