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A prion is an infectious agent composed of protein in a misfolded form. The name prion, is derived from the words protein and infectious. Prions are responsible for the transmissible spongiform encephalopathies in mammals .In humans, prions cause Creutzfeldt-Jakob Disease (CJD) Fatal Familial Insomnia and kuru.
A prion is an infectious agent composed of protein in a misfolded form. The name prion, is derived from the words protein and infectious. Prions are responsible for the transmissible spongiform encephalopathies in mammals .In humans, prions cause Creutzfeldt-Jakob Disease (CJD) Fatal Familial Insomnia and kuru.
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All prion diseases affect the brain or neural tissue and all are currently untreatable.
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The 3haf structure results from a work leaded by Lee S. in 2010, in which they have characterized seven variants of the human prion. The structure was determined by XRAY diffraction in a 2.26-Angstrom resolution.
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A recent study revealed that 1 in 2,000 people in the UK might harbour the infectious prion protein that causes CJD. Human prion is a membrane protein of 16284.86 Da.
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3haf is a domain of the Major prion protein. This domain is between the residue 120 and the 225 of the entire prion .This structure is a succession of helix and sheet beta. The domain contains sites of glycolisation. It can be noticed a mismatch precisely at the residue 129, where a Valin substitutes a Methionin, influencing the susceptibility of the formation of the prion.
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This protein was discovered for the first time in 1960 by an hypothesis witch shows that transmissible spongiform encephlopathies are caused by an infectious agent.
 
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Later, in 1988 the suspected prion was purified by an american professor. This work on prion allows this proffessor to win the Nobel Prize in Physiology or Medicine in 1997
 
==Structure==
==Structure==

Revision as of 17:00, 8 January 2014

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PDB ID 3haf

Drag the structure with the mouse to rotate
3haf, resolution 2.26Å ()
Ligands: ,
Gene: PRNP, PRIP, PRP (Homo sapiens)
Related: 3hak
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Contents

Introduction

A prion is an infectious agent composed of protein in a misfolded form. The name prion, is derived from the words protein and infectious. Prions are responsible for the transmissible spongiform encephalopathies in mammals .In humans, prions cause Creutzfeldt-Jakob Disease (CJD) Fatal Familial Insomnia and kuru.

The 3haf structure results from a work leaded by Lee S. in 2010, in which they have characterized seven variants of the human prion. The structure was determined by XRAY diffraction in a 2.26-Angstrom resolution.

3haf is a domain of the Major prion protein. This domain is between the residue 120 and the 225 of the entire prion .This structure is a succession of helix and sheet beta. The domain contains sites of glycolisation. It can be noticed a mismatch precisely at the residue 129, where a Valin substitutes a Methionin, influencing the susceptibility of the formation of the prion.


Structure

The only description of the structure of prion protein was given by an american team leaded by S.LEE in 2010. In this part, this paper will be our main reference about the conformational diversity in prion protein.

The structure of the 3HAF prion can be determined using X RAY diffraction with a resolution of 2.26 Angstrom. The normal form of the protein is called PrPC and is found in the membrane of cells. It is a 209 amino acids protein with one disulfide bond ans an helical structure.

For this prion, two glycosylated sites exist on helix 2 and 3 at Asn181 and Asn197. A disulfide bond exist between Cys179 and helix 2 ans the other between Cys214 and helix3.

Image:Structure Human Prion.jpg

This protein can bond 2 ligand, Cd2+ (cadnium ions) and Cl- (chloride ion). But, this rotein can also binds a Cu2+ ions on this NH2 tail and this bond can induce conformational change with a lot of unknown effect. The common Methionine/Valine polymorphism t residue in 129 in the PrP influences disease…

Disease

Function

See Also

Reference

  • Lee S, Antony L, Hartmann R, Knaus KJ, Surewicz K, Surewicz WK, Yee VC. Conformational diversity in prion protein variants influences intermolecular beta-sheet formation. EMBO J. 2010 Jan 6;29(1):251-62. Epub 2009 Nov 19. PMID:19927125 doi:10.1038/emboj.2009.333
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