STRUCTURAL FEATURES OF KERATIN AND RELATED INTERMEDIATE FILAMENTS

角蛋白中间体的结构、功能和表达 人和小鼠皮肤的细丝以及相关的中间细丝 其他细胞类型的蛋白质正在研究中。这些研究 旨在了解结构特征，这些结构特征决定了 链的杆域堆积形成细丝芯。现款车型 正在使用电子显微镜方法进行测试， 分析在限制的蛋白水解消化中产生的产物， 完整的丝或它们的亚丝形式。富含甘氨酸的一端 特别是表皮细胞的角蛋白1/10细丝的结构域， 在生物学上是独一无二的。我们认为这些分子组成了一个甘氨酸环 配置.目前的研究旨在确定这些是如何 以及它们如何与其他大分子相互作用， 在表皮组织中表达。人体上的甘氨酸环序列 角蛋白10链在大小和序列上是非常多态。 使用人角蛋白链1和10的基因组克隆，转基因 已经构建了小鼠来检测以下的表达特征： 基因以及在体内探测可能的功能， 链的各个部分，例如杆结构域片段和甘氨酸- 富端域。

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.