COMPLEX BETWEEN DIFFERENTLY PHOSPHORYLATED KINASE DOMAIN OF FGFR1 AND TAMDEN SH2

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 不同磷酸化的FGFR1激动域的结构将有助于更好地了解FGFR1激活的中间状态。为了获得更多的信息，我试图将激活的激酶结构域与天然底物共结晶，该结构域包含两个Src同源结构域(SH2)和磷脂酶C-伽马的C末端延伸(PLCg)。它与蛋白激酶的磷酸化酪氨酸766(PY766)结合，其C端延伸的酪氨酸781(Y781)被反式蛋白激酶磷酸化。这些结构将有助于阐明FGFR1的磷酸化机制，并为通过底物与激酶的结合方式探索下游信号通路提供更多的机会。

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. Structures of differently phosphorylated kinase domain of FGFR1 will give better understanding of intermediate states of FGFR1 activation. To get more information, I try to co-crystallize activated kinase domain with a natural substrate, a domain construct containing two Src Homology domain (SH2) and C-terminal extension of Phospholipase C gamma (PLCg). This binds to phosphorylated tyrosine 766 (pY766) of kinase and its tyrosine 781 (Y781) on C-terminal extension is phosphorylated by kinase in trans. These structures will bring elucidation of phosphorylation mechanism of FGFR1 and give more opportunities to explore the downstream signaling pathways through binding mode between substrate and kinase.