Amyloid precursor protein

Function

Amyloid precursor protein (APP) is a transmembranal protein which is thought to regulate transcription. APP plays a role in synaptic formation and repair.^[1]

Disease

APP is cleaved by β-secretase and the resulting N terminal peptide which is ca. 40 amino acid long is called hAPP β-peptide. The aggregation of the hAPP β-peptide is the cause of Alzheimer’s Disease. For detailed discussion see

• Human APP
  
• Human APP Intracellular Domain Complex with Fe65-PTB2
  
• Beta Amyloid forms Plaques
  
• Amyloid beta

Structural highlights

The extracellular region of APP contains several domains named E1 (residues 1-189) and E2 (residues 346-551). The E1 domain contains a growth factor-like or heparin-binding (residues 28-123) and Cu-binding (residues 124-189) subdomains. Additional domains are: Kunitz-type protease inhibitor (residues 287-344) and Zn-binding (residues 672-687). The Z-binding domain is involved in the oligomerizatin of APP.

3D structures of amyloid precursor protein

Amyloid precursor protein 3D structures