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. 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

spinqualitylabelsall models Human amyloid precursor protein heparin-binding domain 1mwp Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image