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 旨在了解决定杆如何 链的结构域堆积以形成长丝芯。 我们已经使用 交联研究，以确定分子长度和最近的 相邻的分子排列。 一种检测方法， 合成肽已被设计来探索的特点， 灯丝模型。 富含甘氨酸的末端区域，尤其是角蛋白 1/10的表皮细胞细丝在生物学上是独特的。 我们认为 它们组成甘氨酸环构型。 目前的研究是 旨在确定它们是如何包装的以及它们如何相互作用 与表皮组织中共表达的其它大分子。 甘氨酸- 人角蛋白10链上的环状序列 在大小和序列上具有多态性。 利用基因克隆技术 角蛋白链1和10，转基因小鼠已建成检查 基因的表达特征以及体内探针 链的各个部分（例如杆）的可能功能 结构域片段和富含甘氨酸的末端结构域。

The structure, function and expression of the kertin 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 determine how the rod domains of the chains pack to form the filament core. We have used cross-linking studies to determine molecular lengths and the nearest neighbor molecular alignments in the filaments. An assay involving synthetic peptides has been designed to explore the features of the filament models. 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 coexpressed 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.