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Prion
From Proteopedia
Michal Harel (Talk | contribs)
(New page: Crystal Structure of human prion 3haf {{STRUCTURE_3haf| PDB=3haf | SIZE=300| SCENE= |right|CAPTION=human prion 3haf }} '''Prion''' (PrP) is ...)
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Revision as of 11:24, 28 March 2011
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| human prion 3haf | |||||||||
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| Ligands: | , | ||||||||
| Gene: | PRNP, PRIP, PRP (Homo sapiens) | ||||||||
| Related: | 3hak | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Prion (PrP) is a protein which becomes infectious upon undergoing conformation change to an amyloid form, which is self-propagating and become resistant to protease degradation. The fungus Podospora anserine has a prion-like protein HET-S which undergoes a conformation change to amyloid form which prevents its colony from merging with non-compatible colonies. Yeast prion proteins are Sup35 and Ure2. The images at the left and at the right correspond to one representative prion, i.e. the crystal structure of human prion (2haf).
