NMR Structure of Membrane Proteins of T. maritima

T. maritima 膜蛋白的 NMR 结构

• 批准号: 6646340
• 负责人: Linda M Columbus
• 金额: $ 4.16万
• 依托单位: SCRIPPS RESEARCH INSTITUTE, THE
• 依托单位国家: 美国
• 财政年份: 2003
• 资助国家: 美国
• 起止时间: 2003-06-16 至 2006-06-15
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6646340
• 关键词: Archaea; bacterial proteins; circular dichroism; conformation; functional /structural genomics; membrane proteins; nuclear magnetic resonance spectroscopy; polymerase chain reaction; postdoctoral investigator; protein purification; protein structure function; proteomics; site directed mutagenesis

DESCRIPTION (provided by applicant): Membrane protein structure determination is a difficult task for structural biologists. Membrane proteins comprise 30% of the proteome. However, only ~30 unique structures have been determined, making their contribution to the protein data bank less than 0.5%. The majority of membrane proteins are transmembrane helical bundles, but of the known structures roughly half are beta-barrel proteins, which are limited to the outer membrane of bacteria, mitochondria, and chloroplasts. This study targets helical membrane proteins with two, three, and four predicted transmembrane segments for NMR structure determination in order to significantly diversify the different types of membrane protein structures known. Defective membrane proteins have been identified in many diseases due to misfolding and loss of function making them targets for drug design. Structural information could advance the effectiveness of these drug pursuits. In addition, more helical transmembrane structures will aid in the understanding of membrane protein stability and increase the likelihood of predicting membrane protein structures.

描述（由申请人提供）：膜蛋白结构测定对于结构生物学家来说是一项艰巨的任务。膜蛋白占蛋白质组的 30%。然而，仅确定了约 30 个独特结构，使得它们对蛋白质数据库的贡献不到 0.5%。大多数膜蛋白是跨膜螺旋束，但已知结构中大约一半是β-桶蛋白，仅限于细菌、线粒体和叶绿体的外膜。本研究针对具有两个、三个和四个预测跨膜片段的螺旋膜蛋白进行核磁共振结构测定，以显着多样化已知的不同类型的膜蛋白结构。由于错误折叠和功能丧失，在许多疾病中已发现有缺陷的膜蛋白，这使得它们成为药物设计的目标。结构信息可以提高这些药物研究的有效性。此外，更多的螺旋跨膜结构将有助于理解膜蛋白的稳定性并增加预测膜蛋白结构的可能性。