THE MOLECULAR STRUCTURE OF COLLAGEN TYPES I AND II

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目和 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 对于中心来说，它不一定是研究者的机构。 I 型胶原蛋白是动物界中最丰富的单一胶原蛋白，也是大多数哺乳动物结缔组织的重要组成部分。 II 型胶原蛋白是哺乳动物软骨、椎间盘和其他组织发育过程中的重要组成部分，但人们对这两种胶原蛋白在亚纤维水平上的组织知之甚少。幸运的是，在大鼠尾腱和七鳃鳗组织中发现的纤维状 I 型和 II 型胶原蛋白具有一定程度的结晶性，这一特性允许通过 X 射线纤维衍射研究胶原蛋白分子结构。 从大鼠尾腱和几种七鳃鳗组织获得的衍射图案包含有关胶原蛋白链的亚纤维组织的信息，这是本研究感兴趣的特定水平。此前，此类数据（在 BioCAT 收集）用于将 I 型胶原蛋白的 3D 结构解析至 1.1 nm，揭示了胶原酶（和其他 EM 活性分子）结合胶原蛋白链的机制的重要限制。冷冻技术的后续发展将用于扩展该结构的分辨率，同时使用 BioCAT 光束线新开发的微焦点功能收集 II 型胶原蛋白的数据，以类似地使用 MIR 解析其结构。

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. Type I collagen is the single most abundant collagen in the animal kingdom and a critical part of most mammalian connective tissues. Type II collagen is a crucial component of mammalian cartilage, inter-vertebral discs and other tissues during their development, yet relatively little is known concerning the organization of these two collagen types at the sub-fibrillar level. Fortunately, the fibrillar type I and II collagen's found within rat tail tendon and in lamprey tissues are somewhat crystalline, a property that will allow an investigation of collagen molecular structure through X-ray fiber diffraction. Diffraction patterns obtained from both rat tail tendon and several lamprey tissues contain information regarding the sub-fibrillar organization of collagen chains, the specific level of interest to this study. Previously, such data (collected at BioCAT) was used to solve the 3D structure of type I collagen to 1.1 nm, revealing important constraints on the mechanism by which collagenase (and other EM active molecules) bind the collagen chains. Subsequent developments in cryo-freezing techniques will be used to extend the resolution of this structure, whilst data is collected for type II collagen using the newly developed micro-focus capabilities of the BioCAT beamline to similarly solve its structure using MIR.