Amyloid precursor protein: Difference between revisions

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* [[Human APP]]<br />
* [[Human APP]]<br />
* [[Human APP Intracellular Domain Complex with Fe65-PTB2]]<br />
* [[Human APP Intracellular Domain Complex with Fe65-PTB2]]<br />
* [[Amyloid beta]].
* [[Beta Amyloid forms Plaques]]<br />
* [[Amyloid beta]]


== Structural highlights ==
== 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.
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.
</StructureSection>
 
==3D structures of amyloid precursor protein==
==3D structures of amyloid precursor protein==
[[Amyloid precursor protein 3D structures]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
{{#tree:id=OrganizedByTopic|openlevels=0|
 
*APP
 
**[[3nyj]], [[3nyl]], [[3umh]], [[3umi]], [[3umk]] – hAPP E2 domain – human<BR />
**[[3ktm]] – hAPP residues 18-190<BR />
**[[1ze7]], [[2bp4]] – hAPP zinc-binding domain – NMR<BR />
**[[2fjz]], [[2fma]] - hAPP residues 133-189<BR />
**[[1owt]] - hAPP residues 133-189 - NMR<BR />
**[[1tkn]] - hAPP residues 460-569 - NMR<BR />
**[[1mwp]] - hAPP heparin-binding domain<br />
 
*hAPP β-peptide
 
**[[1z0q]], [[2beg]] – hAPP β-peptide residues 1-42 – NMR<br />
**[[1amb]], [[1amc]] – hAPP β-peptide residues 1-28 – NMR<br />
**[[1qcm]], [[1qyt]], [[1qwp]], [[1qxc]] – hAPP β-peptide residues 25-35 – NMR<br />
**[[1ba4]], [[1ba6]], [[2lnq]] – hAPP β-peptide residues 1-40 – NMR<br />
**[[1bjb]], [[1bjc]] – hAPP β-peptide residues 1-28 (mutant) – NMR<br />
**[[1nmj]] – APP β-peptide residues 1-28 – rat – NMR<br />
**[[3bae]] – hAPP β-peptide residues 1-28 + antibody<br />
**[[3bkj]] – hAPP β-peptide residues 1-16 + antibody<br />
**[[2roz]] – hAPP β-peptide residues 1-32 + amyloid β A4 precursor protein - NMR<br />
**[[2wk3]] – hAPP β-peptide residues 1-42 + insulin-degrading enzyme<br />
 
*Amyloid precursor protein binary complex


**[[1ze9]] - hAPP zinc-binding domain + Zn – NMR<BR />
**[[2fk1]], [[2fk2]], [[2fk3]], [[2fkl]] - hAPP residues 133-189 + Cu<BR />
**[[3jti]], [[3gci]] – hAPP peptide residues 699-706 + phospholipase A2<BR />
**[[3l81]] - hAPP peptide residues 761-767 + AP-4 complex subunit μ-1<BR />
**[[3ifl]], [[3ifn]], [[3ifo]], [[3ifp]], [[2r0w]] - hAPP peptide residues 672-711 + antibody<BR />
**[[2wk3]] - hAPP residues 672-713 + insulin degrading enzyme<BR />
**[[3dxc]] - hAPP residues 739-770 + Fe65-PTB2<BR />
**[[3dxd]], [[3dxe]] - hAPP residues 739-770 (mutant) + Fe65-PTB2<BR />
**[[2roz]] - hAPP peptide residues 582-704 + Fe65 C terminal<BR />
**[[2otk]] - hAPP residues 672-711 + ZAB3 affibody dimer - NMR<BR />
**[[3l3t]] - hAPP residues 211-267 + mesotrypsin<br />
**[[3l33]] - hAPP residues 290-341 + trypsin-3 (mutant)
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 11:11, 17 March 2019


Function

Amyloid precursor protein (APP) is a transmembranal protein which is thought to regulate transcription. APP plays a role in synaptic formation and repair.[1]

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

Amyloid precursor protein 3D structures


Human amyloid precursor protein heparin-binding domain 1mwp

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ Turner PR, O'Connor K, Tate WP, Abraham WC. Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory. Prog Neurobiol. 2003 May;70(1):1-32. PMID:12927332

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Michal Harel, Alexander Berchansky
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