Sandbox Reserved 1232
From Proteopedia
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The image shown is the average structure produced by NMR constraints. | The image shown is the average structure produced by NMR constraints. | ||
| + | The protein can exist in multiple isoforms, the normal PrPC (cellular), and as Protease resistance PrPRes like the disease-causing PrPSc (scrapie) and an isoform located in mitochondria. | ||
| + | PrP is highly conserved through mammals. Comparison between primates is especially similar, ranging from 92.9-99.6% similarity in amino acid sequences. | ||
| + | The human protein structure consists of a globular domain with three α-helices and a two-strand antiparallel β-sheet, an NH2-terminal tail, and a short COOH-terminal tail. | ||
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| + | A glycophosphatidylinositol (GPI) membrane anchor at the COOH-terminal tethers PrP to cell membranes, and this proves to be integral to the transmission of conformational change; secreted PrP lacking the anchor component is unaffected by the infectious isoform. | ||
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| + | =Structural Highlights= | ||
| + | Other representations of PrP226: <scene name="/12/3456/Sample/1">color representation</scene> and <scene name="/12/3456/Sample/2">a transparent representation</scene> | ||
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</StructureSection> | </StructureSection> | ||
== Function == | == Function == | ||
| - | + | All 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. | |
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== Disease == | == Disease == | ||
| - | + | In PrPC's mutated state, the prion protein contributes to the development of amyloid diseases (misfolded proteins that stick together forming fibrils). Instead of other infectious agents such as viruses, bacteria, parasites, or fungi, prion proteins do not contain any genetic material such as DNA or RNA. Prion diseases can originate spontaneously, genetically or by infection and are comprised entirely of misfolded proteins. When a misfolded prion (PrPSc) enters a host it induces existing, properly folded PrPC’s to fold into the infectious form. | |
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| + | Mutated Prion proteins are associated with a variety of neurodegenerative diseases such as bovine spongiform encephalopathy, chronic wasting disease, Creutzfeldt–Jakob disease, fatal familial insomnia, feline spongiform encephalopathy, Gerstmann–Sträussler–Scheinker syndrome, kuru, scrapie, transmissible mink encephalopathy, ungulate spongiform encephalopathy, and variant Creutzfeldt–Jakob disease. | ||
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| + | The common prion disease in humans is known as Creutzfeldt-Jakob disease. | ||
== Structural Highlights == | == Structural Highlights == | ||
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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. | ||
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| + | Schätzl HM, Da Costa M, Taylor L, Cohen FE, Prusiner SB (January 1995). "Prion protein gene variation among primates". J. Mol. Biol. 245 (4): 362–74. | ||
Current revision
Contents |
Human Prion Protein
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Function
All 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 diseases (misfolded proteins that stick together forming fibrils). Instead of other infectious agents such as viruses, bacteria, parasites, or fungi, prion proteins do not contain any genetic material such as DNA or RNA. Prion diseases can originate spontaneously, genetically or by infection and are comprised entirely of misfolded proteins. When a misfolded prion (PrPSc) enters a host it induces existing, properly folded PrPC’s to fold into the infectious form.
Mutated Prion proteins are associated with a variety of neurodegenerative diseases such as bovine spongiform encephalopathy, chronic wasting disease, Creutzfeldt–Jakob disease, fatal familial insomnia, feline spongiform encephalopathy, Gerstmann–Sträussler–Scheinker syndrome, kuru, scrapie, transmissible mink encephalopathy, ungulate spongiform encephalopathy, and variant Creutzfeldt–Jakob disease.
The common prion disease in humans is known as Creutzfeldt-Jakob disease.
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.
Schätzl HM, Da Costa M, Taylor L, Cohen FE, Prusiner SB (January 1995). "Prion protein gene variation among primates". J. Mol. Biol. 245 (4): 362–74.
