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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.

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. In it's mutated state the prion protein functions in the development of amyloid disease (misfiled proteins that stick together forming fibrils).

Disease

The disease associated with a mutated Prion protein is Spongiform Ecephalopathies. 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.