Major prion protein (PRNP) is a 253-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P04156.
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The mean pLDDT of this model is 64.2 (low overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.
| pLDDT band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 9% |
| 70 to 90 | Confident: backbone generally right | 41% |
| 50 to 70 | Low: treat with caution | 12% |
| Below 50 | Very low: often disordered regions | 39% |
What pLDDT means and how to read it
Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (By similarity). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or Zn(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity)
Monomer and homodimer. Has a tendency to aggregate into amyloid fibrils containing a cross-beta spine, formed by a steric zipper of superposed beta-strands. Soluble oligomers may represent an intermediate stage on the path to fibril formation. Copper binding may promote oligomerization (PubMed:11524679, PubMed:11900542, PubMed:14623188, PubMed:17468747, PubMed:19204296, PubMed:19927125,…
Cell membrane, Golgi apparatus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2OL9 | X-ray | 0.85 Å | A=170-175 |
| 7RVE | EM | 0.85 Å | A=168-176 |
| 7RVC | EM | 1.0 Å | A=168-176 |
| 7RVJ | EM | 1.0 Å | A/B=169-175 |
| 7RVK | EM | 1.0 Å | A=169-175 |
| 7RVL | EM | 1.0 Å | A=168-176 |
| 3MD4 | X-ray | 1.15 Å | A/B=127-132 |
| 3MD5 | X-ray | 1.4 Å | A/B=127-132 |
| 4E1H | X-ray | 1.4 Å | A/C/E/G/I/K=177-182, B/D/F/H/J/L=211-216 |
| 6PQA | X-ray | 1.46 Å | A=119-124 |
| 4KML | X-ray | 1.5 Å | A=24-231 |
| 4N9O | X-ray | 1.5 Å | A=90-231 |
| 6PQ5 | X-ray | 1.5 Å | A/B=113-118 |
| 3NHC | X-ray | 1.57 Å | A/B=127-132 |
| 3HAK | X-ray | 1.8 Å | A=125-227 |
| 3HEQ | X-ray | 1.8 Å | A/B=90-231 |
| 3NVF | X-ray | 1.8 Å | A=138-143 |
| 3HER | X-ray | 1.85 Å | A/B=90-231 |
| 3NHD | X-ray | 1.92 Å | A/B=127-132 |
| 1I4M | X-ray | 2.0 Å | A=119-226 |
Showing 20 of 70 experimental structures (best resolution first).
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