Prion protein

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
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 a natively unstructured N-terminal region, and a predominantly α-helical C-terminal region from residues ~120-230. 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 of PrP<sup>C</sup>=
=Structure of PrP<sup>C</sup>=
Line 13: Line 13:
=Selected PrP structures=
=Selected PrP structures=
 +
All structures determined by NMR unless otherwise specified
==Human PrP==
==Human PrP==
-
* [[1QLX]] HuPrP 23-230 Average 125-228
+
* [[1QLX]] HuPrP 23-230
-
* [[1QM0]] HuPrP 90-230 Average 125-228
+
* [[1QM0]] HuPrP 90-230
-
* [[1QM2]] HuPrP 121-230 Average 125-228
+
* [[1QM2]] HuPrP 121-230
-
* [[1I4M]] HuPrP 119-226 (X-ray) 119-226
+
* [[1I4M]] HuPrP 119-226 (X-ray)
* [[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
-
* 1FKC HuPrP,E200K 90-231 Average 125-231
+
* [[1FKC]] HuPrP,E200K residues 90-231 (genetic prion disease)
-
* 1H0L HuPrP,M166C,E221C 121-230 20 structures 119-230
+
* [[1H0L]] HuPrP residues 121-230, with an additional disulphide bond analogous to the homolog Doppel
==Other PrPs==
==Other PrPs==
* XXXX Mouse PrP determined by NMR
* XXXX Mouse PrP determined by NMR
- 
* [[1B10]] Syrian hamster PrP 90-231 NMR ensemble of 25 structures
* [[1B10]] Syrian hamster PrP 90-231 NMR ensemble of 25 structures
* [[1DWY]] Cow PrP 121-230 Average 124-227
* [[1DWY]] Cow PrP 121-230 Average 124-227
-
* [[1UW3]] Sheep PrP
+
* [[1UW3]] Sheep PrP (X ray)
* XXXX Frog PrP
* XXXX Frog PrP
* XXXX Chicken PrP
* XXXX Chicken PrP

Revision as of 14:20, 10 December 2008

The prion protein (PrP) is a cell surface glycoprotein. The cellular isoform (PrPC) has a natively unstructured N-terminal region, and a predominantly α-helical C-terminal region from residues ~120-230. PrPC can undergo a structural conversion to a β-sheet rich conformation, termed PrPSc. 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 PrPSc, which arise from autocatalytic refolding of PrPC in a template-dependent manner.

Contents

Structure of PrPC

PDB ID 1hjm

Drag the structure with the mouse to rotate
1hjm, 1 NMR models ()
Related: 1e1g, 1e1j, 1e1p, 1e1s, 1e1u, 1e1w, 1hjn
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



The structure is highly conserved amongst mammals...

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

Models of PrPSc structure

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

Selected PrP structures

All structures determined by NMR unless otherwise specified

Human PrP

  • 1QLX HuPrP 23-230
  • 1QM0 HuPrP 90-230
  • 1QM2 HuPrP 121-230
  • 1I4M HuPrP 119-226 (X-ray)
  • 1E1J HuPrP,M166V 125-228 Average 125-228
  • 1E1S HuPrP,S170N 125-228 Average 125-228
  • 1E1W HuPrP,R220K 125-228 Average 125-228
  • 1FKC HuPrP,E200K residues 90-231 (genetic prion disease)
  • 1H0L HuPrP residues 121-230, with an additional disulphide bond analogous to the homolog Doppel

Other PrPs

  • XXXX Mouse PrP determined by NMR
  • 1B10 Syrian hamster PrP 90-231 NMR ensemble of 25 structures
  • 1DWY Cow PrP 121-230 Average 124-227
  • 1UW3 Sheep PrP (X ray)
  • XXXX Frog PrP
  • XXXX Chicken PrP
  • XXXX Turtle PrP

References

Retrieved from "http://52.214.119.220/wiki/index.php/Prion_protein"
Personal tools