› 2ysz

Solution NMR

Solution structure of the chimera of the C-terminal PID domain of Fe65L and the C-terminal tail peptide of APP

Released:
DOI: 10.2210/pdb2ysz/pdb
PDB entry 2ysz coloured by chain, ensemble of 20 models, front view.
PDB entry 2ysz coloured by chain, ensemble of 20 models, side view.
PDB entry 2ysz coloured by chain, ensemble of 20 models, top view.
Source organism: Mus musculus
Primary publication:
Structure of the C-terminal phosphotyrosine interaction domain of Fe65L1 complexed with the cytoplasmic tail of amyloid precursor protein reveals a novel peptide binding mode.
Li H, Koshiba S, Hayashi F, Tochio N, Tomizawa T, Kasai T, Yabuki T, Motoda Y, Harada T, Watanabe S, Inoue M, Hayashizaki Y, Tanaka A, Kigawa T, Yokoyama S
J Biol Chem 283 27165-78 (2008)
PMID: 18650440

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190092 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amyloid beta precursor protein binding family B member 2 Chain: A
Molecule details ›
Chain: A
Length: 185 amino acids
Theoretical weight: 20.01 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
  • Canonical: Q9DBR4 (Residues: 582-704; Coverage: 16%)
Gene names: Apbb2, Fe65l, Fe65l1
Sequence domains: Phosphotyrosine interaction domain (PTB/PID)
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Not provided

Quick links

Citations

4 review citations

Direct binding of cholesterol to the amyloid precursor protein: An important interaction in lipid-Alzheimer's disease relationships?
Beel et al. (2010)
3 more