Amyloid precursor protein
From Proteopedia
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**[[3l33]] - hAPP residues 290-341 + trypsin-3 (mutant) | **[[3l33]] - hAPP residues 290-341 + trypsin-3 (mutant) | ||
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[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 09:39, 2 December 2015
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| Human amyloid precursor protein heparin-binding domain 1mwp | |||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
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
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
Updated on 02-December-2015
