Miller E J
Ann N Y Acad Sci. 1985;460:1-13. doi: 10.1111/j.1749-6632.1985.tb51152.x.
Although collagen molecules are designed primarily to serve as constituents of supporting aggregates in various tissues, they are present as a relatively large family of proteins that exhibit a wide diversity in structural and chemical features. Molecular diversity is, of course, specified primarily by the different genes for synthesis of the various collagen chains. However, intracellular post-translational modifications of the nascent chains as well as extracellular processing of newly assembled molecules contribute to, and considerably amplify, the diversity specified by the genome. Moreover, the nature of the aggregates derived from various molecular species of collagen reflects this diversity. In this fashion, a great deal of chemical and biological variation is created in otherwise highly similar molecules such as those classified here as belonging to group 1. It is anticipated that further developments regarding these and other molecular species of collagen will considerably refine our understanding of the spectrum of structure and function associated with this unique family of proteins.
尽管胶原蛋白分子主要作为各种组织中支撑聚集体的成分，但它们以相对较大的蛋白质家族形式存在，这些蛋白质在结构和化学特征上表现出广泛的多样性。当然，分子多样性主要由合成各种胶原链的不同基因决定。然而，新生链的细胞内翻译后修饰以及新组装分子的细胞外加工也对基因组所决定的多样性有贡献，并显著放大了这种多样性。此外，源自各种胶原分子种类的聚集体的性质也反映了这种多样性。通过这种方式，在原本高度相似的分子中产生了大量的化学和生物学变异，比如这里归类为第1组的那些分子。预计关于这些以及其他胶原分子种类的进一步发展将极大地完善我们对与这个独特蛋白质家族相关的结构和功能谱的理解。
