DETERMINATION OF FHA STRUCTURE

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。 PIP3是参与信号转导和膜转运的重要第二信使。在海马神经元中，PIP3在轴突顶端的聚集启动了轴突的指定和神经元的极性形成。Gakin是一种类似激动素的运动蛋白，它直接与PIP3相互作用的蛋白相互作用，并介导含有PIP3的囊泡的运输。Gakin中的结合位点定位于FHA结构域编码的一个小区域。我们试图确定FHA结构域在天然形式和复杂形式下的三维结构，以揭示Gakin与PIP3的结合机制。

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. PIP3 is an important second messenger implicated in signal transduction and membrance transport. In hippocampal neurons, the accumulation of PIP3 athe tip of neurite initiastes the axon specification and neuronal polarity fomation. GAKIN, a kinesin-like motor protein, directly interats with a PIP3-interacting protein and mediates the transport of PIP3-Containing vesicles. The binding site in GAKIN was localized to a small region encoded by the FHA domain. We try to determine the 3D structure of FHA domain in its native form and complex form in order to reveal the binding mechanism between GAKIN and PIP3.