Prion protein: Difference between revisions

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The prion protein (PrP) is a cell surface glycoprotein. The cellular isoform (PrP<sup>C</sup>) has two dominas: an dN-terminal region that is natively unstructured, and a C-terminal region from residues ~120-230, which is predominantly α-helical. PrP<sup>C</sup> can undergo a structural conversion to a β-sheet rich conformation, termed PrP<sup>Sc</sup>. Prion diseases such as Creutzfeldt Jakob disease (CJD) in people, and bovine spongiform encephalopathy (BSE) commonly known as "mad cow" disease, are characterterized by aggregates of PrP<sup>Sc</sup>, which arise from autocatalytic refolding of PrP<sup>C</sup> in a template-dependent manner.
The prion protein (PrP) is a cell surface glycoprotein. The cellular isoform (PrP<sup>C</sup>) has two dominas: an dN-terminal region that is natively unstructured, and a C-terminal region from residues ~120-230, which is predominantly α-helical. PrP<sup>C</sup> can undergo a structural conversion to a β-sheet rich conformation, termed PrP<sup>Sc</sup>. Prion diseases such as Creutzfeldt Jakob disease (CJD) in people, and bovine spongiform encephalopathy (BSE) commonly known as "mad cow" disease, are characterterized by aggregates of PrP<sup>Sc</sup>, which arise from autocatalytic refolding of PrP<sup>C</sup> in a template-dependent manner.
Structure from  a


  's normal cellular function is debated, and "knockout" mice lacking PrP are phenotypically normal.
==Structure of PrP<sup>C</sup>==


has a predominantly α-helical structure and is localized to the outer leaflet of the cell membrane by a glycolipid anchor. In prion diseases PrPC undergoes a major structural transformation converting . This process is autocatalytic with PrPSc driving the refolding of PrPC in a template-dependent manner, leading to accumulation of PrPSc and ultimately neuronal cell death.
{{STRUCTURE_1hjm |  PDB=1hjm  |  SCENE= }}
 
==Structure of PrPC==


{{STRUCTURE_1hjm |  PDB=1hjm  |  SCENE=  }}
The structure is highly conserved amongst mammals...


The X-ray structure of sheep PrP was dimeric...


==Models of PrP<sup>Sc</sup> structure==
There are a number of technical obstacles in determining the molecular structure of PrP(sup)Sc</sup>


==Selected PrP structures==
==Selected PrP structures==
=Human PrP=
=Human PrP=
* 1QLX HuPrP                23-230 Average            125-228
* [[1QLX]] HuPrP                23-230 Average            125-228
* 1QM0 HuPrP                90-230 Average            125-228
* [[1QM0]] HuPrP                90-230 Average            125-228
* 1QM2 HuPrP              121-230 Average            125-228
* [[1QM2]] HuPrP              121-230 Average            125-228
* 1I4M HuPrP              119-226 (X-ray)            119-226
* [[1I4M]] HuPrP              119-226 (X-ray)            119-226
* 1E1J HuPrP,M166V        125-228 Average            125-228
* [[1E1J]] HuPrP,M166V        125-228 Average            125-228
* 1E1S HuPrP,S170N        125-228 Average            125-228
* 1E1S HuPrP,S170N        125-228 Average            125-228
* 1E1W HuPrP,R220K        125-228 Average            125-228
* 1E1W HuPrP,R220K        125-228 Average            125-228
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1UW3 Sheep PrP
1UW3 Sheep PrP
* XXXX Frog PrP
* XXXX Frog PrP
* Chicken PrP
* XXXX Chicken PrP
* Turtle PrP
* XXXX Turtle PrP
 
==References==
Retrieved from "https://proteopedia.org/Prion_protein"