Treble clef finger - a functionally diverse zinc-binding structural motif
Treble clef finger - a functionally diverse zinc-binding structural motif
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DOI：
10.1093/nar/29.8.1703
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发表时间：
2001-04-15
影响因子：
14.9
通讯作者：
Grishin, NV
中科院分区：
文献类型：
--
作者：
Grishin, NV
对小蛋白质的相似性检测尤其困难，因此许多蛋白质之间的联系仍未被发现。几种金属结合蛋白的结构和序列分析揭示了SCOP中被分类为不同蛋白质折叠的结构域的意外相似性，并表明属于两个蛋白质类的7个折叠的统一。常见的基序，在本研究中被称为“三叉指”，形成蛋白质结构核心，长度为25-45个残基。三叉指基序围绕中心锌离子组装，由锌节、环、p -发夹和a-螺旋组成，节节和螺旋的第一次转动分别包含两个锌配体。该结构域构成了许多结构的核心，如核糖体蛋白L24E和S14，环指，蛋白激酶半胱氨酸富结构域，核受体样指，LIM结构域，磷脂酰肌醇-3-磷酸结合结构域和His-Me指内切酶。该结构域是一个独特的多功能基模，适用于各种功能。这个具有25个残基结构核心的小结构域可以容纳8个不同的金属结合位点，并且可以具有多种类型的功能，从结合核酸，蛋白质和小分子到催化磷酸二酯键水解，高音clef motif经常被合并在较大的结构中或以双偶体出现。目前的分析表明，在具有不同功能特性的蛋白质中，高音谱号基序定义了一种独特的结构折叠，并形成了主要的锌指基团之一。
Detection of similarity is particularly difficult for small proteins and thus connections between many of them remain unnoticed. Structure and sequence analysis of several metal-binding proteins reveals unexpected similarities in structural domains classified as different protein folds in SCOP and suggests unification of seven folds that belong to two protein classes. The common motif, termed treble clef finger in this study, forms the protein structural core and is 25-45 residues long, The treble clef motif is assembled around the central zinc ion and consists of a zinc knuckle, loop, P-hairpin and an a-helix, The knuckle and the first turn of the helix each incorporate two zinc ligands. Treble clef domains constitute the core of many structures such as ribosomal proteins L24E and S14, RING fingers, protein kinase cysteine-rich domains, nuclear receptor-like fingers, LIM domains, phosphatidylinositol-3-phosphate-binding domains and His-Me finger endonucleases, The treble clef finger is a uniquely versatile motif adaptable for various functions. This small domain with a 25 residue structural core can accommodate eight different metal-binding sites and can have many types of functions from binding of nucleic acids, proteins and small molecules, to catalysis of phosphodiester bond hydrolysis, Treble clef motifs are frequently incorporated in larger structures or occur in doublets. Present analysis suggests that the treble clef motif defines a distinct structural fold found in proteins with diverse functional properties and forms one of the major zinc finger groups.