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. PACSIN 1 is a neuron specific protein that plays a center role in synaptic vesicle endocytosis of neuron cells. PACSIN I contains two well-defined domains. The N-terminal F-BAR domain has been shown to play an important role in vesicle formation and related membrane remodeling events. Low resolution TEM study indicates the F-BAR domain can self-assembly and form a protein coat on the membrane surface and constrain its geometry. The C-terminal SH3 domain can bind with NWASP and Dynamin, which are key proteins involved in vesicle formation and the transportation. Our research is trying to use the crystallographic study to understand its function and regulation at the atomic level. The obtained crystal structures will serve as the first high-resolution models to investigate its membrane binding, regulation and activation mechanisms. The onsite activities will be including 1) screen and test crystals quality;2) Collect datasets on good quality crystals and process the data 3) Solve the protein structures based on qualified datasets.
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