Prions are misfolded proteins with the ability to transmit their misfolded shape onto normal variants of the same protein. They characterize several fatal and transmissible neurodegenerative diseases in humans and many other animals. It is not known what causes the normal protein to misfold, but the abnormal three-dimensional structure is suspected of conferring infectious properties, collapsing nearby protein molecules into the same shape. The word prion derives from "proteinaceous infectious particle". The hypothesized role of a protein as an infectious agent stands in contrast to all other known infectious agents such as viroids, viruses, bacteria, fungi, and parasites, all of which contain nucleic acids (DNA, RNA, or both). Prion isoforms of the prion protein (PrP), whose specific function is uncertain, are hypothesized as the cause of transmissible spongiform encephalopathies (TSEs), including scrapie in sheep, chronic wasting disease (CWD) in deer, bovine spongiform encephalopathy (BSE) in cattle (commonly known as "mad cow disease") and Creutzfeldt–Jakob disease (CJD) in humans. All known prion diseases in mammals affect the structure of the brain or other neural tissue; all are progressive, have no known effective treatment, and are always fatal. Here you can see the structure of the C-terminal domain of a prion protein from mouse, determined by X-ray crystallography (PDB code: 1DWY)
#molecularart ... #immolecular ... #prion ... #neurodegeneration ... #folding ... #xray
Prion protein rendered with @proteinimaging and composed by @corelphotopaint
#molecularart ... #immolecular ... #prion ... #neurodegeneration ... #folding ... #xray
Prion protein rendered with @proteinimaging and composed by @corelphotopaint
