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: 8170165
• 负责人: Eun-Young Kim
• 金额: $ 0.03万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-05-01 至 2011-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8170165
• 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; 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 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 C-terminus.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 （1）线粒体在能量代谢，钙信号传导，衰老和细胞死亡方面起着核心作用。 尽管它们的重要性，但到目前为止，只有很少的线粒体膜蛋白结构得到了解决。我们结晶了人类线粒体蛋白之一，并希望执行衍射实验以解决其结构。所得的结构将阐明这些线粒体膜蛋白如何发挥其功能。 （2）电压门控钙通道（CAVS）是多支亚基大分子，可在膜去极化后控制钙进入细胞的钙。钙调蛋白（CAM）通过与CAV C末端的关联在钙依赖性调节中起关键作用。 尽管已经对CAV-CAM相互作用进行了大量功能研究，但CAM调节的结构细节尚不清楚。 为了阐明CAV调节的结构基础，我们在具有不同长度的CAM结合基序的复合物中制备了不同CAM状态的晶体。