Chen J M, Sheldon A, Pincus M R
Department of Chemistry, osteoArthritis Sciences, Inc., Cambridge, MA 02139, USA.
J Biomol Struct Dyn. 1995 Jun;12(6):1129-59. doi: 10.1080/07391102.1995.10508804.
A procedure is described for constructing a three-dimensional model of fibril-forming human type II collagen based on the "Smith" microfibril model. This model is a complex of five individual collagen triple-helical molecules, and is based on known structural parameters for collagen. Both experimental and theoretical data were used as constraints to guide the modeling. The resulting fibril model for type II collagen is in agreement with both physical and chemical characteristics produced by experimental staining patterns of type II fibrils. Some advantages of the type II model are that the stereochemistry of all the sidechain groups is accounted for, and specific atomic interactions can now be studied. This model is useful for: development of therapeutics for collagen related diseases; development of synthetic collagen tissues; design of chemical reagents (i.e., tanning agents) to treat collagen-related products; and study of the structural and functional aspects of type II collagen. Described is the procedure by which the Smith microfibril of type II collagen was developed using molecular modeling tools, validation of the model by comparison to electron-microscopic images of fibril staining patterns, and some applications of this microfibril model.
描述了一种基于“史密斯”微原纤维模型构建形成原纤维的人II型胶原蛋白三维模型的方法。该模型是五个单独的胶原蛋白三螺旋分子的复合体，基于胶原蛋白已知的结构参数。实验数据和理论数据均用作约束条件来指导建模。所得的II型胶原蛋白原纤维模型与II型原纤维实验染色模式产生的物理和化学特征均相符。II型模型的一些优点在于考虑了所有侧链基团的立体化学，并且现在可以研究特定的原子相互作用。该模型可用于：开发治疗胶原蛋白相关疾病的疗法；开发合成胶原蛋白组织；设计用于处理胶原蛋白相关产品的化学试剂（即鞣剂）；以及研究II型胶原蛋白的结构和功能方面。描述了使用分子建模工具开发II型胶原蛋白史密斯微原纤维的过程、通过与原纤维染色模式的电子显微镜图像比较对模型进行验证以及该微原纤维模型的一些应用。
