› 1y15

Solution NMR

Mouse Prion Protein with mutation N174T

Released:
DOI: 10.2210/pdb1y15/pdb
PDB entry 1y15 coloured by chain, ensemble of 20 models, front view.
PDB entry 1y15 coloured by chain, ensemble of 20 models, side view.
PDB entry 1y15 coloured by chain, ensemble of 20 models, top view.
Source organism: Mus musculus
Primary publication:
Prion protein NMR structures of elk and of mouse/elk hybrids.
Gossert AD, Bonjour S, Lysek DA, Fiorito F, Wüthrich K
Proc Natl Acad Sci U S A 102 646-50 (2005)
PMID: 15647363

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138267 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 112 amino acids
Theoretical weight: 13.25 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P04925 (Residues: 120-231; Coverage: 48%)
Gene names: Prn-p, 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
Refinement method: torsion angle dynamics
Expression system: Escherichia coli BL21

Quick links

Citations

35 review citations

Polyproline-II helix in proteins: structure and function.
Adzhubei et al. (2013)
34 more

5 mentions without citation

A structural overview of the vertebrate prion proteins.
Pastore et al. (2007)
4 more