Prion

From Proteopedia
Revision as of 11:24, 28 March 2011 by Michal Harel (talk | contribs) (New page: left|200px|thumb|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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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).

File:3haf.png
Crystal Structure of human prion 3haf
Drag the structure with the mouse to rotate
human prion 3haf
Ligands: CD, CL
Gene: PRNP, PRIP, PRP (Homo sapiens)
Related: 3hak
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel, Joel L. Sussman