› 2m8t

Solution NMR

Solution NMR structure of the V209M variant of the human prion protein (residues 90-231)

Released:
DOI: 10.2210/pdb2m8t/pdb
PDB entry 2m8t coloured by chain, ensemble of 20 models, front view.
PDB entry 2m8t coloured by chain, ensemble of 20 models, side view.
PDB entry 2m8t coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Thermodynamic stabilization of the folded domain of prion protein inhibits prion infection in vivo.
Kong Q, Mills JL, Kundu B, Li X, Qing L, Surewicz K, Cali I, Huang S, Zheng M, Swietnicki W, Sönnichsen FD, Gambetti P, Surewicz WK
Cell Rep 4 248-54 (2013)
PMID: 23871665

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: 146 amino acids
Theoretical weight: 16.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04156 (Residues: 90-231; Coverage: 62%)
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: 79%
Refinement method: simulated annealing, molecular dynamics, MOLECULAR DYNAMICS
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Structural mechanisms of oligomer and amyloid fibril formation by the prion protein.
Sengupta et al. (2018)
13 other articles

1 mention without citation

Thermodynamic stabilization of the folded domain of prion protein inhibits prion infection in vivo.
Kong et al. (2013)