EXAMINING THE MECHANISM OF ACTION OF RECEPTOR TYROSINE KINASES (RTKS) AND THE CE

检查受体酪氨酸激酶 (RTKS) 和 CE 的作用机制

• 批准号: 8363384
• 负责人: JOSEPH SCHLESSINGER
• 金额: $ 0.48万
• 依托单位: BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-07-01 至 2012-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8363384
• 关键词: Biological; Complex; Crystallography; Disease; FGFR1 gene; FGFR2 gene; FRS2 gene; Functional disorder; Funding; Goals; Grant; Laboratories; Light; Molecular; National Center for Research Resources; Nucleic Acid Regulatory Sequences; Phosphotransferases; Principal Investigator; Receptor Protein-Tyrosine Kinases; Research; Research Infrastructure; Resources; Signal Pathway; Signal Transduction; Source; Structure; Synchrotrons; System; United States National Institutes of Health; X-Ray Crystallography; cost; phospholipase C gamma; protein tyrosine kinase PYK2; structural biology

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. The major goal of the laboratory is to elucidate the mechanism of action of receptor tyrosine kinases (RTKs) and the cellular signaling pathways that they activate in order to understand how this cell signaling system is regulated under normal biological conditions or in diseases caused by dysfunction in RTKs and their signaling pathways. One of our aims is to apply X-ray crystallography in order to obtain a molecular view of the mechanism of action of RTKs and key components of their signaling pathways.Two of the structural biology projects currently being pursued in our laboratory:1.) Analysis of the structure of different activated phosphorylated forms of FGFR1 and FGFR2 kinase domains in complex with phospholipase-C-gamma or FRS2[SMALL_ALPHA].2.) Analysis of the FAT and FERM domains, two regulatory regions of the protein tyrosine kinase PYK2.

该子项目是利用资源的众多研究子项目之一 由 NIH/NCRR 资助的中心拨款提供。子项目的主要支持 并且子项目的首席研究员可能是由其他来源提供的， 包括其他 NIH 来源。 子项目可能列出的总成本 代表子项目使用的中心基础设施的估计数量， NCRR 赠款不直接向子项目或子项目工作人员提供资金。 该实验室的主要目标是阐明受体酪氨酸激酶（RTK）的作用机制及其激活的细胞信号传导通路，以了解该细胞信号传导系统在正常生物条件下或在因功能障碍引起的疾病中如何受到调节。 RTK 及其信号通路。 我们的目标之一是应用 X 射线晶体学，以获得 RTK 作用机制及其信号通路关键组成部分的分子视图。我们实验室目前正在进行的两个结构生物学项目：1.) 分析与磷脂酶-C-gamma 或 FRS2[SMALL_ALPHA] 复合的不同活化磷酸化形式的 FGFR1 和 FGFR2 激酶结构域的结构。2.) FAT 和 FERM 分析结构域，蛋白酪氨酸激酶 PYK2 的两个调节区域。