FOCAL ADHESION KINASE 2

粘着斑激酶 2

• 批准号: 7957278
• 负责人: JOSEPH SCHLESSINGER
• 金额: $ 0.79万
• 依托单位: BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-07-01 至 2010-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7957278
• 关键词: Binding; Cells; Computer Retrieval of Information on Scientific Projects Database; Crystallography; Data Collection; Data Set; Disease; Fibroblast Growth Factor Receptors; Focal Adhesions; Funding; Future; Grant; Institution; Light; Malignant Neoplasms; Methionine; PTK2B gene; Phosphorylation; Phosphotransferases; Research; Research Personnel; Resources; Sampling; Signal Pathway; Signal Transduction; Source; Stimulus; Structure; Synchrotrons; Therapeutic; United States National Institutes of Health; Work; insight; interest; molecular dynamics; research study

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. FAK2 is a molecule involved in relaying signals from the outside to the inside of the cell, allowing the cell to respond to external stimuli. As many disfunctions can arise throught the misregulation of such signaling pathways, a further understanding of the molecular dynamics and interactions involved will have serious implications in terms of future therapeutic treatments. We plan to collect full data sets of the FAK2 focal adhesion-targeting and FERM domains as well as co-crystals of these domains bound to their respective substrates. These crystals will be prepared without the usage of any heavy atom derivatives. However, seleno-methionine derivatives may be used and would require MAD data collection. All items/samples brought into the facility will return with us and be properly disposed of. Furthermore, our group is currnetly working on solving the structures of the FGF receptor kinase domain in its various phosphorylated states. Doing so, in combination with binding experiments, will allow us to completely understand the order of activation/phosphorylation of the FGFR kinase and structural reasons behind the order of phosphorylation. FGFR is involved in numerous disorders and cancers, and such insight as to its mode of activation is of extreme scientific interest.

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。 FAK2是一种参与从外部到细胞内部传递信号的分子，使细胞对外部刺激有反应。由于许多失调可能会通过这种信号通路的不利调节而产生，因此对所涉及的分子动力学和相互作用的进一步理解将对未来的治疗治疗产生严重的影响。我们计划收集FAK2焦点粘附和FERM域的完整数据集，以及这些域与其各自底物约束的共结晶。这些晶体将在不使用任何重原子衍生物的情况下制备。但是，可以使用硒蛋白衍生物，并且需要疯狂的数据收集。所有带入该设施的物品/样品将与我们一起返回并得到适当处理。此外，我们的小组正在努力求解其各种磷酸化状态中FGF受体激酶结构域的结构。这样做，结合结合实验，将使我们能够完全理解FGFR激酶的激活/磷酸化顺序以及磷酸化顺序背后的结构原因。 FGFR参与了许多疾病和癌症，其激活方式的见解具有极大的科学利益。