Parkin is an E3 ubiquitin ligase protein involved in the ubiquitin-...

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Parkin is an E3 ubiquitin ligase protein involved in the ubiquitin-proteosome system that mediates the targeting of proteins for degradation. Mutations in parkin, which disrupt the catalytic activity, lead to the accumulation of toxic substrates that damage dopaminergic neurons, causing the autosomal recessive form of Parkinson’s disease. Parkin is considered to be a neuroprotectant, due to its role in eliminating these toxic substrates. Recent structures have revealed much about its regulation and function, but the structure of the active form remains unknown. It has been shown through ITC and fluorescence polarization experiments that phosphorylated ubiquitin can bind between the RING0 and IBR domain of parkin, believed to be a key point in the activation. From the inactive structures in the PDB and literature please predict the active structure of parkin. Experimentally, how can we validate the structural prediction of the active form?

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The parkin protein has low basal activity in vitro. The most common state is autoinhibited state, but based on the structure it can be determined how it is activated. It is biologically very important because it is included in the following processes: autophagy of damaged mitochondria, cell survival pathways and vesicle trafficking. The mutation of different sites can lead to the observation of the active site and forms. Selective mutation allows determination of...

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