› 1skh

Solution NMR

N-terminal (1-30) of bovine Prion protein

Released:
DOI: 10.2210/pdb1skh/pdb
PDB entry 1skh coloured by chain, ensemble of 22 models, front view.
PDB entry 1skh coloured by chain, ensemble of 22 models, side view.
PDB entry 1skh coloured by chain, ensemble of 22 models, top view.
Source organism: Bos taurus
Primary publication:
NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein.
Biverståhl H, Andersson A, Gräslund A, Mäler L
Biochemistry 43 14940-7 (2004)
PMID: 15554701

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145256 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 30 amino acids
Theoretical weight: 3.42 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P10279 (Residues: 1-30; Coverage: 3%)
Gene names: PRNP, PRP
Sequence domains: Major prion protein bPrPp - N terminal

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this NMR entry.
Refinement method: DYANA torsion angle dynamics, simulated annealing

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Citations

6 review citations

The magic of bicelles lights up membrane protein structure.
Dürr et al. (2012)
5 more

1 mention without citation

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Bigot et al. (2018)