Cysteine and histidine shuffling: mixing and matching cysteine and histidine residues in zinc finger proteins to afford different folds and function
Cysteine and histidine shuffling: mixing and matching cysteine and histidine residues in zinc finger proteins to afford different folds and function
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DOI：
10.1039/c1dt11071c
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发表时间：
2011-01-01
影响因子：
4
通讯作者：
Michel, Sarah L. J.
中科院分区：
文献类型：
--
作者：
Michalek, Jamie L.;Besold, Angelique N.;Michel, Sarah L. J.
锌指蛋白利用锌用于结构目的：锌以四面体配位几何结构结合半胱氨酸和组氨酸配体的组合，促进蛋白质折叠和功能。虽然对经典的锌指蛋白质有很多了解，其利用Cys（2）His（2）配体组来配位锌并折叠成反平行β折叠/α螺旋折叠，但还有13个其他家族的“非经典”锌指蛋白质，其金属配位与蛋白质结构/功能之间的关系较少定义。这篇文章的重点是两类非经典的锌指蛋白：Cys（3）His型锌指蛋白和Cys（2）His（2）Cys型锌指蛋白。这些蛋白以四面体几何形状结合锌，就像经典的锌指蛋白一样，但它们采用完全不同的折叠并靶向不同的寡核苷酸。我们目前的理解之间的关系，配体集，金属离子，折叠和功能的这些非经典的锌指进行了讨论。
Zinc finger proteins utilize zinc for structural purposes: zinc binds to a combination of cysteine and histidine ligands in a tetrahedral coordination geometry facilitating protein folding and function. While much is known about the classical zinc finger proteins, which utilize a Cys(2)His(2) ligand set to coordinate zinc and fold into an anti-parallel beta sheet/alpha helical fold, there are thirteen other families of 'non-classical' zinc finger proteins for which relationships between metal coordination and protein structure/function are less defined. This 'Perspective' article focuses on two classes of these non-classical zinc finger proteins: Cys(3)His type zinc finger proteins and Cys(2)His(2)Cys type zinc finger proteins. These proteins bind zinc in a tetrahedral geometry, like the classical zinc finger proteins, yet they adopt completely different folds and target different oligonucleotides. Our current understanding of the relationships between ligand set, metal ion, fold and function for these non-classical zinc fingers is discussed.