› 2lp1

Solution NMR

The solution NMR structure of the transmembrane C-terminal domain of the amyloid precursor protein (C99)

Released:
DOI: 10.2210/pdb2lp1/pdb
PDB entry 2lp1 coloured by chain, ensemble of 30 models, front view.
PDB entry 2lp1 coloured by chain, ensemble of 30 models, side view.
PDB entry 2lp1 coloured by chain, ensemble of 30 models, top view.
Source organism: Homo sapiens
Primary publication:
The amyloid precursor protein has a flexible transmembrane domain and binds cholesterol.
Barrett PJ, Song Y, Van Horn WD, Hustedt EJ, Schafer JM, Hadziselimovic A, Beel AJ, Sanders CR
Science 336 1168-71 (2012)
PMID: 22654059

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138353 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
C99 Chain: A
Molecule details ›
Chain: A
Length: 122 amino acids
Theoretical weight: 13.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05067 (Residues: 671-770; Coverage: 13%)
Gene names: A4, AD1, APP
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 43%
Refinement method: molecular dynamics, simulated annealing
Expression system: Escherichia coli

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Citations

78 review citations

Excitotoxicity: bridge to various triggers in neurodegenerative disorders.
Mehta et al. (2013)
77 more

18 mentions without citation

Molecular dynamics simulations of biological membranes and membrane proteins using enhanced conformational sampling algorithms.
Mori et al. (2016)
17 more