CRYSTAL STRUCTURES OF ION CHANNEL, SERPIN COMPLEXES, AND OTHERS

离子通道、丝氨酸蛋白酶抑制剂复合物等的晶体结构

• 批准号: 8362198
• 负责人: PAUL CURMI
• 金额: $ 0.03万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-03-01 至 2012-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8362198
• 关键词: Chloride Channels; Complex; Docking; Funding; Grant; Harvest; Ion Channel; Ion Channel Protein; Light; Membrane; National Center for Research Resources; Principal Investigator; Proteins; Radiation; Research; Research Infrastructure; Resolution; Resources; Serpins; Source; Spliceosomes; Structure; System; Telomerase; United States National Institutes of Health; Work; base; cost; degradosome; protein complex; structural biology

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. The CLIC proteins constitute a new class of chloride ion channel proteins which exist in both a soluble and integral membrane forms. We have solved the structures of five CLIC proteins in the soluble form and a structurally distinct membrane docking form of CLIC1. We aim is to determine the structure of the integral membrane form as well as protein complexes. The Sm/Lsm proteins form the basis for many RNPs (including the spliceosome, telomerase and degradosome). We have solved three homomeric Sm/Lsm ring complexes and we are currently working on heteroheptameric Lsm structures as well as RNP complexes. Cryptophytes have a unique light harvesting system. We have solved the structures of PE545 at 0.97 ¿ resolution and PC645 at 1.4 ¿ resolution. Each of these 50kD proteins diffract to much higher resolution PE545 0.86¿ & PC645

该子项目是利用资源的众多研究子项目之一 由 NIH/NCRR 资助的中心拨款提供。子项目的主要支持 并且子项目的主要研究者可能是由其他来源提供的， 包括其他 NIH 来源。 子项目可能列出的总成本 代表子项目使用的中心基础设施的估计数量， NCRR 赠款不直接向子项目或子项目工作人员提供资金。 CLIC蛋白构成一类新的氯离子通道蛋白，其以可溶性和完整膜形式存在。 我们已经解析了五种可溶形式的 CLIC 蛋白的结构以及结构上不同的 CLIC1 膜对接形式。 我们的目标是确定完整膜形式以及蛋白质复合物的结构。 Sm/Lsm 蛋白构成了许多 RNP（包括剪接体、端粒酶和降解体）的基础。我们已经解决了三个同聚 Sm/Lsm 环复合物，目前正在研究异七聚 Lsm 结构以及 RNP 复合物。 隐植物具有独特的光收集系统。 我们已经解析了 0.97 ¡ 分辨率的 PE545 和 1.4 ¡ 分辨率的 PC645 的结构。 这些 50kD 蛋白质中的每一个都可衍射至更高分辨率的 PE545 0.86¿ 和 PC645