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: 7954247
• 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: 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/7954247
• 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; structural biology; synchrotron radiation

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。 可溶性蛋白进入内质网中的分泌途径，然后移至高尔基体综合体。如果他们没有特定的分类信息，他们将退出高尔基体并分泌给细胞外部。因此，摆脱了大量流程？两者都要求可溶性蛋白带有信号，并且整体膜受体蛋白识别信号并将可溶性蛋白拉入囊泡，以将其携带到其他目的地。某种程度上，在植物高尔基体中，一个受体（BP80）识别一种信号，并将一种可溶性蛋白拉入裂解液泡途径中，而不同的受体（RMR）识别出不同的信号并将不同的可溶性蛋白吸入蛋白质储存液途径。除裂解途径受体外，哺乳动物高尔基体复合物中发生了类似的过程。为了理解这种复杂但决定性的分类机制，我们决定解决受体分子的晶体结构。