Computer model of a bovine type I collagen microfibril
Computer model of a bovine type I collagen microfibril
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DOI：
10.1093/protein/9.1.43
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发表时间：
1996-01-01
期刊：
影响因子：
--
通讯作者：
Chen, JM
中科院分区：
文献类型：
--
作者：
King, G;Brown, EM;Chen, JM
胶原蛋白是细胞外基质的结构蛋白家族，形成原纤维的胶原蛋白是皮肤、软骨、骨、血管壁和内部器官的主要结构蛋白，除了生物学功能之外，胶原蛋白还提供用于医学、食品和皮革工业的天然结构框架。将I型胶原蛋白组织成三螺旋的许多方案，在过去的30年中，已经提出了微原纤维和原纤维。这里，描述了牛I型胶原“Smith”微原纤维的分子模型的开发。在横截面中，该模型显示出五个三螺旋的对称的五边形分组。该模型包含15条每条具有315个残基的多肽链，该模型足够大以允许将其总体结构特征与通过电子显微镜获得的染色胶原的图像进行比较，但又足够小以在小型计算机或工作站上操作。（其中包括）研究胶原蛋白的结构-功能关系，探索折叠途径，预测潜在交联剂或化学修饰的功效，并设计用于特定应用的合成胶原样材料或修饰。
Collagens are a family of structural proteins of the extracellular matrix, The fibril-forming collagens are the major structural proteins of skin, cartilage, bone, blood vessel walls and internal organs, In addition to biological function, the collagens provide natural structural frameworks that are utilized in the medical, food and leather industries, Many schemes for the organization of type I collagen into triple helices, microfibrils and fibrils have been proposed during the past 30 years, Here, the development of a molecular model of a bovine type I collagen 'Smith' microfibril is described, In cross-section, this model exhibits a symmetrical, pentagonal grouping of five triple helices, The model comprises 15 polypeptide chains having 315 residues each, This model is large enough to allow a comparison of its gross structural features with images of stained collagen obtained by electron microscopy, yet small enough to be manipulated on a minicomputer or workstation, The model is useful for (among others) studies of structure-function relationships in collagen, exploring folding pathways, predicting the efficacy of potential crosslinking agents or chemical modifications, and designing synthetic collagen-like materials or modifications for specific applications.