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Contents 1 Human Prion Protein 2 Function 3 Disease 4 Relevance 5 Structural Highlights 6 References

Human Prion Protein

spinqualitylabelsall models PrP226* - Solution-state NMR structure of truncated human prion protein (PDB entry 5l6r) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Structure The image shown is the average structure produced by NMR constraints. The protein can exist in multiple isoforms, the normal PrPC, and as Protease resistance PrPRes like the disease-causing PrPSc(scrapie) and an isoform located in mitochondria.

Function

Mammals contain cellular prion related proteins (PrPC) in their bodies and when functioning correctly are believed to assist in copper binding and signal transduction in neurons. Expression of the protein is most predominant in the nervous system but occurs in many other tissues throughout the body.

Disease

In PrPC's mutated state, the prion protein contributes to the development of amyloid disease (misfolded proteins that stick together forming fibrils). Mutated Prion proteins are associated with a variety of neurodegenerative diseases such as

The common prion disease in humans is known as Creutzfeldt-Jakob disease.

Relevance

Structural Highlights

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

References

An, Lu, David Fitzpatrick, and Paul M Harrison. "Emergence And Evolution Of Yeast Prion And Prion-Like Proteins." BMC Evolutionary Biology 16.(2016): 24.MEDLINE Complete. Web. 12 Feb. 2017.

Kovacs, Gabor G., and Herbert Budka. “Prion Diseases: From Protein to Cell Pathology.” The American Journal of Pathology 172.3 (2008): 555–565. PMC. Web. 13 Feb. 2017.