STRUCTURAL STUDIES OF MITOCHONDRIAL MEMBRANE PROTEINS AND CA-DEPENDENT REGULATIO

线粒体膜蛋白的结构研究和 CA 依赖性调节

• 批准号: 7954507
• 负责人: Eun-Young Kim
• 金额: $ 0.06万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-03-01 至 2010-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7954507
• 关键词: Aging; Binding; Calcium; Calcium Channel; Calcium Signaling; Calmodulin; Cell Death; Cells; Complex; Computer Retrieval of Information on Scientific Projects Database; Energy Metabolism; Funding; Grant; Human; Institution; Length; Light; Membrane; Mitochondria; Mitochondrial Membrane Protein; Mitochondrial Proteins; Play; Regulation; Research; Research Personnel; Resources; Role; Source; Structure; United States National Institutes of Health; base; macromolecule; research study; structural biology; synchrotron radiation; voltage

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. (1) Mitochondria play a central in role energy metabolism, calcium signaling, aging, and cell death. Despite their importance, only few structures of mitochondrial membrane protein have been solved so far. We crystallized one of the human mitochondrial proteins and wish to perform diffraction experiments to solve its structure. The resulting structure will shed a light on how these mitochondrial membrane proteins exert their functions. (2) Voltage-gated calcium channels (Cavs) are multi-subunit macromolecules that control calcium entry into cells upon membrane depolarization. Calmodulin (CaM) plays a critical role in calcium-dependent modulation of CaVs through association with the Cav ?1 C-terminus. Although a multitude of functional studies of the CaV-CaM interaction have been carried out, the structural details of CaM modulation of CaVs remain unclear. To elucidate the structural basis of CaV regulation, we have prepared crystals of different CaM states in complexes with different lengths of CaM binding motifs from CaV ?1 C-terminus.

这个子项目是众多研究子项目之一