Amyloid precursor protein: Difference between revisions
Michal Harel (talk | contribs) New page: {{STRUCTURE_3ktm| PDB=3ktm | SIZE=300| SCENE= |right| CAPTION=Human amyloid precursor protein E1-dimer domain, 3ktm }} '''Amyloid precursor protein''' (APP) is thought to ... |
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<StructureSection load='1mwp' size='350' side='right' scene='45/455464/Cv/1' caption='Human amyloid precursor protein heparin-binding domain [[1mwp]]'> | |||
== Function == | |||
'''Amyloid precursor protein''' (APP) is thought to regulate transcription. | '''Amyloid precursor protein''' (APP) is a transmembranal protein which is thought to regulate transcription. APP plays a role in synaptic formation and repair.<ref>PMID:12927332</ref> | ||
== 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<br /> | |||
* [[Human APP]]<br /> | |||
* [[Human APP Intracellular Domain Complex with Fe65-PTB2]]<br /> | |||
* [[Beta Amyloid forms Plaques]]<br /> | |||
* [[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== | ==3D structures of amyloid precursor protein== | ||
[[Amyloid precursor protein 3D structures]] | |||
</StructureSection> | |||
== References == | |||
<references/> | |||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Latest revision as of 11:11, 17 March 2019
FunctionAmyloid precursor protein (APP) is a transmembranal protein which is thought to regulate transcription. APP plays a role in synaptic formation and repair.[1] DiseaseAPP 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 highlightsThe 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 proteinAmyloid precursor protein 3D structures
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