DETERMINATION OF FHA STRUCTURE

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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.