Amyloid precursor protein

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   Print3D 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

3D structures of amyloid precursor protein

Updated on 17-March-2019

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• APP
  • Human APP, Human APP Intracellular Domain Complex with Fe65-PTB2, Beta Amyloid forms Plaques, Amyloid beta, Amyloid precursor protein 3D structures – hAPP E2 domain – human
    
  • 4pwq, 3ktm - hAPP E1 domain
    
  • 3ktm – hAPP residues 18-190
    
  • 1ze7, 2bp4 – hAPP zinc-binding domain – NMR
    
  • 2fjz, 2fma - hAPP residues 133-189
    
  • 1owt - hAPP residues 133-189 - NMR
    
  • 5buo – hAPP residues 351-691
    
  • 1tkn - hAPP residues 460-569 - NMR
    
  • 1mwp, 4pqd - hAPP heparin-binding domain
    
  • 5txd – hAPP residues 698-703
    
  • 5how, 5hox, 5hoy – hAPP residues 698-707 (mutant)
    
  • 5aef – hAPP residues 630-657 – Cryo EM
    
• hAPP β-peptide
  • 1z0q, 2beg – hAPP β-peptide residues 1-42 – NMR
    
  • 5oqv – hAPP -peptide residues 1-42 – Cryo EM
    
  • 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
    
  • 5lfy – hAPP -peptide residues 17-26 – 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, 5c67 - hAPP residues 290-341 + trypsin-3 (mutant)
    
  • 5amb – hAPP residues 706-713 + angiotensin-converting enzyme
    
  • 5am8 – hAPP residues 675-681 + angiotensin-converting enzyme
    

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Michal Harel, Alexander Berchansky