Amyloid precursor protein

spinqualitylabelsall models PDB ID 1mwp Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
Human amyloid precursor protein heparin-binding domain 1mwp
Structural annotation: Resources: CATH : 1Mwpa00 InterPro : Ipr011178, Ipr008155, Ipr008154, Ipr015849, Ipr002223, Ipr013803 Pfam : PF02177 SCOP : d1mwpa_ UniProt : P05067
Functional annotation: Cellular component: extracellular region membrane integral to membrane integral to plasma membrane cell surface coated pit Biological process: endocytosis apoptosis cellular copper ion homeostasis cell adhesion Notch signaling pathway neuromuscular process Molecular function: heparin binding endopeptidase inhibitor activity zinc ion binding protein binding copper ion binding metal ion binding identical protein binding iron ion binding serine-type endopeptidase inhibitor activity binding
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

FunctionFunction

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

DiseaseDisease

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
  
• Amyloid beta.

Structural highlightsStructural 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 protein3D structures of amyloid precursor protein

Updated on 01-November-2015

{"openlevels":0}

• APP
  • 3nyj, 3nyl, 3umh, 3umi, 3umk – hAPP E2 domain – human
    
  • 3ktm – hAPP residues 18-190
    
  • 1ze7, 2bp4 – hAPP zinc-binding domain – NMR
    
  • 2fjz, 2fma - hAPP residues 133-189
    
  • 1owt - hAPP residues 133-189 - NMR
    
  • 1rw6 - hAPP residues 346-551
    
  • 1tkn - hAPP residues 460-569 - NMR
    
  • 1mwp - hAPP heparin-binding domain
    
• hAPP β-peptide
  • 1z0q, 2beg – hAPP β-peptide residues 1-42 – NMR
    
  • 1amb, 1amc – hAPP β-peptide residues 1-28 – NMR
    
  • 1qcm, 1qyt, 1qwp, 1qxc – hAPP β-peptide residues 25-35 – NMR
    
  • 1ba4, 1ba6, 2lnq – hAPP β-peptide residues 1-40 – NMR
    
  • 1bjb, 1bjc – hAPP β-peptide residues 1-28 (mutant) – NMR
    
  • 1nmj – APP β-peptide residues 1-28 – rat – NMR
    
  • 3bae – hAPP β-peptide residues 1-28 + antibody
    
  • 3bkj – hAPP β-peptide residues 1-16 + antibody
    
  • 2roz – hAPP β-peptide residues 1-32 + amyloid β A4 precursor protein - NMR
    
  • 2wk3 – hAPP β-peptide residues 1-42 + insulin-degrading enzyme
    
• Amyloid precursor protein binary complex
  • 1ze9 - hAPP zinc-binding domain + Zn – NMR
    
  • 2fk1, 2fk2, 2fk3, 2fkl - hAPP residues 133-189 + Cu
    
  • 3jti, 3gci – hAPP peptide residues 699-706 + phospholipase A2
    
  • 3l81 - hAPP peptide residues 761-767 + AP-4 complex subunit μ-1
    
  • 3ifl, 3ifn, 3ifo, 3ifp, 2r0w - hAPP peptide residues 672-711 + antibody
    
  • 2wk3 - hAPP residues 672-713 + insulin degrading enzyme
    
  • 3dxc - hAPP residues 739-770 + Fe65-PTB2
    
  • 3dxd, 3dxe - hAPP residues 739-770 (mutant) + Fe65-PTB2
    
  • 2roz - hAPP peptide residues 582-704 + Fe65 C terminal
    
  • 2otk - hAPP residues 672-711 + ZAB3 affibody dimer - NMR
    
  • 3l3t - hAPP residues 211-267 + mesotrypsin
    
  • 3l33 - hAPP residues 290-341 + trypsin-3 (mutant)