Amyloid precursor protein: Difference between revisions

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  {{STRUCTURE_1mwp| PDB=1mwp | SIZE=400| SCENE= |right|  CAPTION=Human amyloid precursor protein heparin-binding domain [[1mwp]] }} 
<StructureSection load='1mwp' size='350' side='right' scene='45/455464/Cv/1' caption='Human amyloid precursor protein heparin-binding domain [[1mwp]]'>


'''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<br />
== Function ==
* [[Human APP]]<br />
* [[Human APP Intracellular Domain Complex with Fe65-PTB2]]<br />
* [[Amyloid beta]].


__NOTOC__
'''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> 


==3D structures of amyloid precursor protein==
== Disease ==


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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 />
{{#tree:id=OrganizedByTopic|openlevels=0|
* [[Human APP]]<br />
* [[Human APP Intracellular Domain Complex with Fe65-PTB2]]<br />
* [[Beta Amyloid forms Plaques]]<br />
* [[Amyloid beta]]


*APP
== Structural highlights ==


**[[3nyj]], [[3nyl]], [[3umh]], [[3umi]], [[3umk]] – hAPP E2 domain – human<BR />
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.
**[[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 />
**[[1rw6]] - hAPP residues 346-551<BR />
**[[1tkn]] - hAPP residues 460-569 - NMR<BR />
**[[1qyt]], [[1qwp]], [[1qxc]] - hAPP residues 25-35 – NMR<BR />
**[[1mwp]] - hAPP heparin-binding domain<br />


*hAPP β-peptide
==3D structures of amyloid precursor protein==
 
[[Amyloid precursor protein 3D structures]]
**[[1z0q]], [[2beg]] – hAPP β-peptide residues 1-42 – NMR<br />
**[[1amb]], [[1amc]] – hAPP β-peptide residues 1-28 – NMR<br />
**[[1qcm]], [[1qwp]], [[1qxc]], [[1qyt]] – 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
</StructureSection>


**[[1ze9]] - hAPP zinc-binding domain + Zn – NMR<BR />
== References ==
**[[2fk1]], [[2fk2]], [[2fk3]], [[2fkl]] - hAPP residues 133-189 + Cu<BR />
<references/>
**[[3jti]], [[3gci]] – hAPP peptide + phospholipase A2<BR />
**[[3l81]] - hAPP peptide + AP-4 complex subunit μ-1<BR />
**[[3ifl]], [[3ifn]], [[3ifo]], [[3ifp]], [[2r0w]] - hAPP peptide + antibody<BR />
**[[2wk3]] - hAPP residues 1-42 + 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 + 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)
}}
[[Category:Topic Page]]
[[Category:Topic Page]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky