› 1m25

Solution NMR

STRUCTURE OF SYNTHETIC 26-MER PEPTIDE CONTAINING 145-169 SHEEP PRION PROTEIN SEGMENT AND C-TERMINAL CYSTEINE IN TFE SOLUTION

Released:
DOI: 10.2210/pdb1m25/pdb
PDB entry 1m25 coloured by chain, ensemble of 20 models, front view.
PDB entry 1m25 coloured by chain, ensemble of 20 models, side view.
PDB entry 1m25 coloured by chain, ensemble of 20 models, top view.
Source organism: Ovis aries
Primary publication:
Possible role of region 152-156 in the structural duality of a peptide fragment from sheep prion protein.
Megy S, Bertho G, Kozin SA, Debey P, Hoa GH, Girault JP
Protein Sci 13 3151-60 (2004)
PMID: 15537751

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-540619 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 26 amino acids
Theoretical weight: 3.43 KDa
Source organism: Ovis aries
Expression system: Not provided
UniProt:
  • Canonical: P23907 (Residues: 145-169; Coverage: 11%)
Gene names: PRNP, PRP, SIP

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing using torsion angle dynamics as implemented in the program CNS
Expression system: Not provided

Quick links

Citations

3 review citations

The consequences of pathogenic mutations to the human prion protein.
van der Kamp et al. (2009)
2 more

2 mentions without citation

Possible role of region 152-156 in the structural duality of a peptide fragment from sheep prion protein.
Megy et al. (2004)
1 more