3-DIMENSIONAL SOLUTION STRUCTURE OF A SINGLE ZINC FINGER DNA-BINDING DOMAIN
3-DIMENSIONAL SOLUTION STRUCTURE OF A SINGLE ZINC FINGER DNA-BINDING DOMAIN
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DOI：
10.1126/science.2503871
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发表时间：
1989-08-11
期刊：
影响因子：
56.9
通讯作者：
WRIGHT, PE
中科院分区：
文献类型：
--
作者：
LEE, MS;GIPPERT, GP;WRIGHT, PE
通过核磁共振（NMR）光谱法测定了锌指核酸结合基序的三维溶液结构。光谱的合成肽对应于一个单一的锌指从非洲爪蟾蛋白Xfin产生的距离和二面角的限制，被用来产生结构的距离几何和约束的分子动力学计算。锌指是一个独立折叠的结构域，具有紧凑的球状结构，其中锌原子被两个半胱氨酸和两个组氨酸配体结合。多肽骨架折叠由定义明确的螺旋组成，起始于α。并且以310螺旋结尾，相对于两个β打包。以发夹结构排列的链。在螺旋的暴露面上的高密度的碱性和极性氨基酸侧链可能参与DNA结合。
The three-dimensional solution structure of a zinc finger nucleic acid binding motif has been determined by nuclear magnetic resonance (NMR) spectroscopy. Spectra of a synthetic peptide corresponding to a single zinc finger from the Xenopus protein Xfin yielded distance and dihedral angle constraints that were used to generate structures from distance geometry and restrained molecular dynamics calculations. The zinc finger is an independently folded domain with a compact globular structure in which the zinc atom is bound by two cysteine and two histidine ligands. The polypeptide backbone fold consists of a well-defined helix, starting as .alpha. and ending as 310 helix, packed against two .beta. strands that are arranged in a hairpin structure. A high density of basic and polar amino acid side chains on the exposed face of the helix are probably involved in DNA binding.