CRYSTAL STRUCTURES OF ION CHANNEL, SERPIN COMPLEXES, INTEGRON CARGO, MOLECULAR C

离子通道晶体结构、丝氨酸蛋白酶抑制剂复合物、INTEGRON CARGO、分子 C

• 批准号: 7597913
• 负责人: PAUL CURMI
• 金额: $ 0.02万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-03-01 至 2008-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7597913
• 关键词: Chloride Ion; Class; Complex; Computer Retrieval of Information on Scientific Projects Database; Docking; Funding; Grant; Harvest; Institution; Integrons; Ion Channel; Ion Channel Protein; Light; Membrane; Molecular; Proteins; Research; Research Personnel; Resolution; Resources; Serpins; Source; Spliceosomes; Structure; System; Telomerase; United States National Institutes of Health; Work; base; degradosome

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 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 four 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

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