STRUCTURAL STUDY OF LIGAND BINDING DOMAIN OF A PLANT VACUOLAR SORTING RECEPTOR

植物液泡分选受体配体结合域的结构研究

• 批准号: 7598104
• 负责人: CHULHEE KANG
• 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/7598104
• 关键词: Cells; Complex; Computer Retrieval of Information on Scientific Projects Database; Destinations; Funding; Golgi Apparatus; Grant; IGF Type 2 Receptor; Institution; Ligand Binding Domain; Lytic; Membrane; Pathway interactions; Plants; Process; Proteins; Research; Research Personnel; Resources; Reticulum; Signal Transduction; Sorting - Cell Movement; Source; Structure; United States National Institutes of Health; Vacuole; Vesicle; receptor; sortilin

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. Soluble proteins enter the secretory pathway in the endoplasminc reticulum and then move to the Golgi complex. If they have no specific sorting information on them, they exit the Golgi and are secreted to the cell exterior. Therefore, sorting away from this ¿bulk flow¿ requires both that the soluble protein carries a signal, and that an integral membrane receptor protein recognizes the signal and pulls the soluble protein into a vesicle that will carry it to a different destination. Somehow, within the plant Golgi apparatus, one receptor (BP80) recognizes one type of signal and pulls a soluble protein into the lytic vacuole pathway, while a different receptor (RMR) recognizes a different signal and pulls a different soluble protein into the protein storage vacuole pathway. A similar process occurs in the mammalian Golgi complex, except the lytic pathway receptors are the mannose-6-phosphate receptor and sortilin. In order to understand this complex but decisive sorting mechanism, we have decided to solve the crystal structure of the receptor molecules.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中央赠款提供的资源 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此，在列出的机构中可能会被压制 对于中心，这不一定是调查员的工厂。 可溶性蛋白进入内质蛋白的途径，并在其上移动到高尔基体上。散装流¿都需要可溶性蛋白质携带信号，并且在植物高尔基体中以某种方式将其带入囊泡，将其带到不同的目的地。虽然不同的受体（RMR）将不同的可溶性蛋白拉入蛋白质储存液途径，但裂解途径受体除外是甘露糖-6-磷酸盐记录分类SM，但我们决定解决受体分子的地壳结构。