Prion protein

The prion protein (PrP) is a cell surface glycoprotein. The cellular isoform (PrP^C) is predominantly α-helical, but can undergo a structural conversion to a β-sheet rich conformation, termed PrP^Sc. 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^Sc, which arise from autocatalytic refolding of PrP^C in a template-dependent manner. Structure from a

  's normal cellular function is debated, and "knockout" mice lacking PrP are phenotypically normal.

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 of PrPC

spinqualitylabelsall models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D load='1hjm' size='350' frame='false' scene=
1hjm, 1 NMR models (default scene)
Related:	1e1g, 1e1j, 1e1p, 1e1s, 1e1u, 1e1w, 1hjn
Structural annotation: Resources: CATH : 1Hjma00 InterPro : Ipr000817 Pfam : PF00377 SCOP : d1hjma_ UniProt : P04156
Functional annotation: Cellular component: extrinsic to membrane plasma membrane Golgi apparatus membrane raft cytoplasm membrane endoplasmic reticulum Biological process: protein homooligomerization cellular copper ion homeostasis metabolic process response to oxidative stress Molecular function: copper ion binding protein binding GPI anchor binding tubulin binding microtubule binding
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

PrP structures

1AG2 Mouse PrP 121-231 determined by NMR 1B10 Syrian hamster PrP 90-231 NMR ensemble of 25 structures 1DWY BoPrP 121-230 Average 124-227 1DWZ BoPrP 121-230 20 structures 124-227 1DX0 BoPrP 23-230 Average 124-227 1DX1 BoPrP 23-230 20 structures 124-227 1E1G HuPrP,M166V 125-228 20 structures 125-228 1E1J HuPrP,M166V 125-228 Average 125-228 1E1P HuPrP,S170N 125-228 20 structures 125-228 1E1S HuPrP,S170N 125-228 Average 125-228 1E1U HuPrP,R220K 125-228 20 structures 125-228 1E1W HuPrP,R220K 125-228 Average 125-228 1FKC HuPrP,E200K 90-231 Average 125-231 1FO7 HuPrP,E200K 90-231 30 structures 125-231 1HJM HuPrP Average 1HJN HuPrP 20 structures 1H0L HuPrP,M166C,E221C 121-230 20 structures 119-230 1I4M HuPrP 119-226 (X-ray) 119-226 1QLX HuPrP 23-230 Average 125-228 1QLZ HuPrP 23-230 20 structures 125-228 1QM0 HuPrP 90-230 Average 125-228 1QM1 HuPrP 90-230 20 structures 125-228 1QM2 HuPrP 121-230 Average 125-228 1QM3 HuPrP 121-230 20 structures 125-228 1UW3 OvPrP

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Kurt Giles, Claudio Garutti, Eran Hodis, Joel L. Sussman, Jaime Prilusky, Michal Harel