Eden Yitna Teferedegn1,2*, Batuhan Yesilyurt2 and Cemal Un2
Prion and SOD1 are implicated in a number of cascades of cellular reactions. Though prion is presumed to have multiple cellular functions, the absence of a crystallized form of mutant prion protein and the challenge in finding therapeutic options intimidates the scientific community from disseminating absolute picture of prion protein and prion diseases pathomechanism. In the same way, SOD1 is a critical protein that involves in a many cellular functions. SOD1 is mainly known for its active role in cellular oxidative stress. Superoxide dismutase activity, metal and protein binding and free radical detoxification are of well characterized activities of SOD1 . Both proteins are highly expressed in brain regions specifically in frontal cortex (BA9), Cerebellar hemisphere, NA (Basal ganglia), cerebellum and the like. These proteins assumed to synergistically work in protecting the cell from oxidative stress. Prion binds and provides copper to SOD1 to facilitate the removal of free radicals. Here, CluspPro Server was used to predict the protein-protein interaction between SOD1 and PRNP. Based on ClusPro outputs and free energy values, model 0 was considered as the best possible interaction model of SOD1 and PrP. PyMol Interface Residue script was also used to filter and find all the presumable residues both in SOD1 and prion. Accordingly, some domains of SOD1 were identified to actively interact with prion. Therefore, it is dare to conclude the presence of close connection between prion and SOD1 beyond just functional interaction.
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