› 2l1d

Solution NMR

Mouse prion protein (121-231) containing the substitution Y169G

Released:
DOI: 10.2210/pdb2l1d/pdb
PDB entry 2l1d coloured by chain, ensemble of 20 models, front view.
PDB entry 2l1d coloured by chain, ensemble of 20 models, side view.
PDB entry 2l1d coloured by chain, ensemble of 20 models, top view.
Source organism: Mus musculus
Primary publication:
Cellular prion protein conformation and function.
Damberger FF, Christen B, Pérez DR, Hornemann S, Wüthrich K
Proc Natl Acad Sci U S A 108 17308-13 (2011)
PMID: 21987789

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-138267 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 114 amino acids
Theoretical weight: 13.3 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
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

Quick links

Citations

6 review citations

The formation, function and regulation of amyloids: insights from structural biology.
Landreh et al. (2016)
5 more

2 mentions without citation

The landscape of the prion protein's structural response to mutation revealed by principal component analysis of multiple NMR ensembles.
Gendoo et al. (2012)
1 more