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.
Computational; Disease; Interaction; Prediction; Prion; SOD1