THE MOLECULAR STRUCTURE OF COLLAGEN TYPES I AND II

I 型和 II 型胶原蛋白的分子结构

• 批准号: 8168617
• 负责人: Joseph Patrick Rosen O'Dubhthaigh Orgel
• 金额: $ 6.47万
• 依托单位: ILLINOIS INSTITUTE OF TECHNOLOGY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-01-01 至 2010-12-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8168617
• 关键词: Animals; Binding; Cartilage; Collagen; Collagen Type I; Collagen Type II; Computer Retrieval of Information on Scientific Projects Database; Connective Tissue; Data; Development; Fiber; Freezing; Funding; Grant; Institution; Investigation; Lampreys; Molecular Structure; Pattern; Property; Rattus; Research; Research Personnel; Resolution; Resources; Roentgen Rays; Source; Structure; Tail; Techniques; Tendon structure; Tissues; United States National Institutes of Health; beamline; collagenase; interest; spine bone structure; three dimensional structure

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.

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 I型胶原是动物界中含量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，但对这两种胶原在亚纤维水平上的组织结构知之甚少。幸运的是，在大鼠尾腱和七鳃鳗组织中发现的I型和II型胶原纤维具有一定的结晶性质，这一特性将使我们能够通过X射线纤维衍射来研究胶原分子结构。从鼠尾肌腱和几种七鳃鳗组织获得的衍射图包含关于胶原链的亚纤维组织的信息，这是本研究感兴趣的特定水平。以前，这些数据(在BioCAT收集)被用来解算I型胶原的3D结构到1.1 nm，揭示了胶原酶(和其他EM活性分子)结合胶原链的机制的重要限制。冷冻技术的后续发展将用于扩展这种结构的分辨率，同时使用BioCAT光束线新开发的微聚焦功能收集II型胶原的数据，以类似地使用MIR解决其结构。