Sandbox Reserved 1232
From Proteopedia
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| - | == | + | ==Human Prion Protein== |
<StructureSection load='5l6r' size='350' side='right' caption='PrP226* - Solution-state NMR structure of truncated human prion protein (PDB entry [[5l6r]])' scene=''> | <StructureSection load='5l6r' size='350' side='right' caption='PrP226* - Solution-state NMR structure of truncated human prion protein (PDB entry [[5l6r]])' scene=''> | ||
=Structure= | =Structure= | ||
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| - | </StructureSection>'''Human Prion Protein'' | ||
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| - | + | </StructureSection> | |
== Function == | == 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. | 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. | ||
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
| - | </StructureSection> | ||
== References == | == 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. | 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. | 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. | ||
Revision as of 19:35, 24 April 2017
Contents |
Human Prion Protein
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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.
