› 2kun

Solution NMR

Three dimensional structure of HuPrP(90-231 M129 Q212P)

Released:
DOI: 10.2210/pdb2kun/pdb
PDB entry 2kun coloured by chain, ensemble of 20 models, front view.
PDB entry 2kun coloured by chain, ensemble of 20 models, side view.
PDB entry 2kun coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
NMR structure of the human prion protein with the pathological Q212P mutation reveals unique structural features.
Ilc G, Giachin G, Jaremko M, Jaremko Ł, Benetti F, Plavec J, Zhukov I, Legname G
PLoS One 5 e11715 (2010)
PMID: 20661422

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137455 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 148 amino acids
Theoretical weight: 16.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04156 (Residues: 90-231; Coverage: 62%)
Gene names: ALTPRP, PRIP, PRNP, PRP
Sequence domains: Prion/Doppel alpha-helical domain
Structure domains: Prion/Doppel protein, beta-ribbon domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 90%
Refinement method: torsion angle dynamics, simulated annealing
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Allosteric function and dysfunction of the prion protein.
Linden et al. (2012)
8 more

9 mentions without citation

Probing early misfolding events in prion protein mutants by NMR spectroscopy.
Giachin et al. (2013)
8 more