STRUCTURAL FEATURES OF KERATIN AND RELATED INTERMEDIATE FILAMENTS

角蛋白中间体的结构、功能及表达 人和鼠皮肤的细丝及其相关的中间细丝 其他细胞类型的蛋白质，正在进行研究。这些研究是 旨在了解决定 链条的杆状结构域堆积形成丝状核心。当前型号 正在使用电子显微镜方法以及通过 有限蛋白水解法产生的产物分析 完整的丝状物或亚丝状物。富含甘氨酸的一端 特别是表皮细胞角蛋白1/10细丝的结构域是 生物学上独一无二的。我们认为这些物质组成了一个甘氨酸环 配置。目前的研究旨在确定这些 以及它们可能如何与其他大分子共同作用- 在表皮组织中表达。人体上的甘氨酸环序列 角蛋白10链在大小和序列上具有极大的多态。 利用基因组克隆人角蛋白链1和10，转基因 已经构建了小鼠来检测其表达特征 以及在体内探索该基因的可能功能 链的不同部分，如杆状结构域片段和甘氨酸- 丰富的端域。

The structure, function and expression of the keratin intermediate filaments of human and mouse skin, and the related intermediate filament proteins of other cell types, are being investigated. These studies are designed to understand the structural features that determined how the rod domains of the chains pack to form the filament core. Current models are being tested using electron microscopic methods as well as by analysis of the products generated on limited proteolytic digestion of intact filaments or subfilamentous forms of them. The glycine-rich end domains of especially the keratin 1/10 filaments of epidermal cells are unique in biology. We believe these organize into a glycine-loop configuration. Current studies are designed to determine how these are packed and how they might interact with other macromolecules co- expressed in epidermal tissues. The glycine loop sequences on the human keratin 10 chain are extraordinarily polymorphic in size and sequence. Using genomic clones to the human keratin chains 1 and 10, transgenic mice have been constructed to examine the expression characteristics of the genes as well as to probe in vivo the likely functions of the various portions of the chains, such as rod domain segments and glycine- rich end domains.