Prion
From Proteopedia
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human prion domain swapped dimer complex with Cd and Cl ions 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 becomes 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). For more details see Prion protein. Click here to see (morph was taken from Gallery of Morphs of the Yale Morph Server.
Contents |
3D structures of prion
Update December 2011
PrP short polypeptides
3nve – ShPrP residues 138 -143 – Syrian hamster
2kkg - PrP residues 23 -106 – Golden hamster - NMR
3nvf – hPrP residues 138 -143 – human
2ol9 - hPrP residues 170 – 175
3nhc, 3nhd, 3md4, 3md5 - hPrP residues 127 – 132
2iv5 - hPrP residues 173 -195 – NMR
1oei - hPrP residues 61 - 84 – NMR
1oeh - hPrP residues 61 - 68 – NMR
2iv6 - hPrP residues 173 -195 (mutant) – NMR
2iv4 - hPrP residues 180 -195 – NMR
3nvg, 3nvh - mPrP residues 138 -143 – mouse
1skh - bPrP residues 1 – 30 - bovine
3fva - ePrP residues 173 -178 – Elk
1s4t - sPrP residues 135 – 155 – sheep – NMR
1m25 - sPrP residues 152 – 156 – NMR
1g04 - sPrP residues 145 – 169 – NMR
2rmv, 2rmw - sPrP residues 142 – 166 (mutant) – NMR
PrP
3o79 – rPrP C-terminal – rabbit
2fj3 - rPrP C-terminal – NMR
2joh, 2jom - rPrP C-terminal (mutant) – NMR
1xyw – ePrP C terminal - NMR
2ku4 - PrP C-terminal – horse
3fva - ePrP C-terminal – NMR
2kfl - PrP C-terminal – Wallaby – NMR
2k56 - PrP C-terminal – Vole – NMR
2ktm – sPrP residues 167-234 H2H3 domain (mutant) – NMR
1xyu, 1y2s - sPrP C-terminal – NMR
1uw3 - sPrP C-terminal
3haf, 3hak, 3hj5, 1i4m - hPrP C-terminal
1hjm, 1hjn, 2kun – hPrP C-terminal – NMR
1h0l, 1fkc, 2k1d, 1fo7, 1e1s, 1e1g, 1e1j, 1e1p, 1e1u, 1e1w, 1qlx, 1qlz, 1qm0, 1qm1, 1qm2, 1qm3, 1qlz, 1qm0, 1qm1, 2lej- hPrP C-terminal (mutant) - NMR
3heq, 3her, 3hes, 3hjx - hPrP C-terminal (mutant)
2ku5, 2ku6, 2kfm, 2kfo, 2k5o, 1y16, 1y15 - mPrP C-terminal (mutant)
1xyx - mPrP C-terminal
2l1k, 2l1d, 2l1e, 2l40 - mPrP C terminal (mutant) – NMR
1ag2, 2l1h, 2l39 - mPrP C terminal - NMR
1u3m – PrP C-terminal – chicken – NMR
1u5l - PrP C-terminal – turtle – NMR
1xu0 - PrP C-terminal – frog – NMR
1xyj - PrP C-terminal – cat – NMR
1xyk - PrP C-terminal – dog – NMR
1xyq - PrP C-terminal – pig – NMR
1dwy, 1dx0, 1dx1 - bPrP C-terminal – NMR
1dwz - bPrP C-terminal (mutant) - NMR
1b10 - ShPrP C-terminal – NMR
2lh8 - ShPrP C-terminal + thiamine – NMR
Yeast prions
2onx, 2olx – Sup35 residues 8 - 11 – yeast
2omm, 1yjo, 1yjp – Sup35 residues 7 – 13
1jzr, 1k0a, 1k0b, 1k0c, 1k0d – Ure2p + glutathione derivartive
1g6w, 1g6y – Ure2p globular domain
1hqo – Ure2p nitrogen regulation fragment
PrP+antibody
2w9e - hPrP C-terminal + anti-PrP antibody
2hh0 - bPrP peptide epitope + anti-PrP antibody
1cu4 - ShPrP peptide epitope + anti-PrP antibody
1tpx, 1tqb, 1tqc - sPrP C-terminal + anti-PrP antibody
HET-S from Podospora anserine
2kj3, 2rnm – HET-S C-terminal – NMR
2wvn, 2wvo - HET-S N-terminal
2wvq - HET-S N-terminal (mutant)