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.

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