› 5yj5

Solution NMR

structure for wildtype Human prion protein (M129)

Released:
DOI: 10.2210/pdb5yj5/pdb
PDB entry 5yj5 coloured by chain, ensemble of 20 models, front view.
PDB entry 5yj5 coloured by chain, ensemble of 20 models, side view.
PDB entry 5yj5 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for the complete resistance of the human prion protein mutant G127V to prion disease.
Zheng Z, Zhang M, Wang Y, Ma R, Guo C, Feng L, Wu J, Yao H, Lin D
Sci Rep 8 13211 (2018)
PMID: 30181558

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: 142 amino acids
Theoretical weight: 16.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli-Pichia pastoris shuttle vector pPpARG4
UniProt:
  • Canonical: P04156 (Residues: 91-231; Coverage: 61%)
Gene names: ALTPRP, PRIP, PRNP, PRP
Sequence domains: Prion/Doppel alpha-helical domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 78%
Refinement method: simulated annealing
Expression system: Escherichia coli-Pichia pastoris shuttle vector pPpARG4

Quick links

Citations

2 review citations

Insight From Animals Resistant to Prion Diseases: Deciphering the Genotype - Morphotype - Phenotype Code for the Prion Protein.
Myers et al. (2020)
1 more

9 mentions without citation

The Action of Chemical Denaturants: From Globular to Intrinsically Disordered Proteins.
Paladino et al. (2023)
8 more