Amyloid precursor protein

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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

Amyloid precursor protein (APP) is thought to regulate transcription. 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.

3D structures of amyloid precursor protein3D structures of amyloid precursor protein

Updated on 09-April-2013

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
1qyt, 1qwp, 1qxc - hAPP residues 25-35 – NMR
1mwp - hAPP heparin-binding domain

hAPP β-peptidehAPP β-peptide

1z0q, 2beg – hAPP β-peptide residues 1-42 – NMR
1amb, 1amc – hAPP β-peptide residues 1-28 – NMR
1qcm, 1qwp, 1qxc, 1qyt – 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 complexAmyloid precursor protein binary complex

1ze9 - hAPP zinc-binding domain + Zn – NMR
2fk1, 2fk2, 2fk3, 2fkl - hAPP residues 133-189 + Cu
3jti, 3gci – hAPP peptide + phospholipase A2
3l81 - hAPP peptide + AP-4 complex subunit μ-1
3ifl, 3ifn, 3ifo, 3ifp, 2r0w - hAPP peptide + antibody
2wk3 - hAPP residues 1-42 + insulin degrading enzyme
3dxc - hAPP residues 739-770 + Fe65-PTB2
3dxd, 3dxe - hAPP residues 739-770 (mutant) + Fe65-PTB2
2roz - hAPP peptide + 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)