THE MOLECULAR STRUCTURE OF COLLAGEN TYPES I AND II

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得主要资金， 因此可以在其他CRISP条目中表示。所列机构为 中心，不一定是研究者的机构。 纤维胶原是动物细胞外基质（ECM）的基本成分，形成所有已知哺乳动物结缔组织的结构基础：骨骼、皮肤、角膜、牙齿、肌腱、结扎线、血管和淋巴管以及包括心脏和肺的所有器官系统。然而，尽管胶原蛋白具有基本的生物学重要性，但对胶原蛋白的一般知识理解仅限于其三螺旋“二级”结构或整个原纤维的重金属染色电子显微镜图像。然而，从细胞和生物医学的角度来看，胶原蛋白结构的重要方面是在中间亚原纤维水平，其中许多重要的生物过程发生在生长中，发展和疾病。这些包括但不限于：原纤维形成，正常生长和发育期间和运动后的组织重塑，以及形成器官系统、骨骼、软骨等的支架，也就是动物的身体是建立在显然，获得胶原蛋白分子（结缔组织内）的明确和上下文可视化对科学界具有重要价值。因此，本提案的目的是：1）通过纤维晶体学对II型和I型纤维状胶原进行结构表征。2)通过纤维晶体学和生物信息学/计算方法，从结构上表征通常与胶原蛋白复合的细胞外基质分子的分子结构。3）开发纤维晶体学和微X射线衍射（<$XD）技术，提高成功完成目标1和2的机会。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The fibrous collagens are the fundamental constituents of the Extracellular Matrix (ECM) of animals, forming the structural basis of all known mammalian connective tissue: bones, skin, cornea, teeth, tendons, ligature, blood and lymphatic vessels and all organ systems including the heart and lungs. Yet, despite the fundamental biological importance of collagen, the general-knowledge understanding of collagen is limited to its triple-helical 'secondary' structure or of the heavy metal stained electron microscopy images of whole fibrils A significant aspect of collagen structure from a cellular and biomedical point of view, however, is at the intermediate sub-fibrillar level, where many important biological processes occur in growth, development and disease. These include but are not limited to: fibrillogenesis, tissue remolding during normal growth and development and following exercise, and in forming the scaffolding upon which organ systems, bones, cartilage, etc., i.e. the animal body, are built upon. Clearly, obtaining an unambiguous and contextualized visualization of collagen molecules (within connective tissue) would be of significant value to the scientific community. Therefore, the aims of this proposal are to: 1) To structurally characterize the fibrillar collagens types II and I by fiber crystallography. 2) To structurally characterize the molecular organization of extracellular matrix molecules commonly found complexed with the collagens via fiber crystallography and bioinformatics / computational methods.3) To develop fiber crystallography and Micro X-ray Diffraction (¿XD) techniques that enhances the chance of successful completion of aims 1 and 2.