Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, Maryland 21201-1180, USA.
Dalton Trans. 2011 Dec 21;40(47):12619-32. doi: 10.1039/c1dt11071c. Epub 2011 Sep 26.
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.
锌与半胱氨酸和组氨酸配体结合，形成四面体配位几何结构，从而促进蛋白质折叠和功能。虽然人们对经典的锌指蛋白有了很多了解，这些蛋白利用 Cys(2)His(2)配体来配位锌，并折叠成反平行的β片/α螺旋折叠，但还有另外 13 种“非经典”锌指蛋白家族，其金属配位与蛋白质结构/功能之间的关系定义不明确。本文主要介绍这两类非经典锌指蛋白：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，与经典锌指蛋白类似，但它们采用完全不同的折叠方式，靶向不同的寡核苷酸。本文讨论了我们目前对这些非经典锌指蛋白中配体、金属离子、折叠和功能之间关系的理解。
