Amyloid precursor protein: Difference between revisions

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

Michal Harel, Alexander Berchansky

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-   {{STRUCTURE_3ktm|  PDB=3ktm  | SIZE=300| SCENE= |right|   CAPTION=Human amyloid precursor protein E1-dimer domain complex with butane diol, sulfate and acetate, [[3ktm]] }}
+<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.  For detailed discussion see [[Human APP]] and [[Human APP Intracellular Domain Complex with Fe65-PTB2]].
+== Function ==
-{{TOC limit|limit=2}}
+'''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 ==
+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]]
-''Update November 2011''
+== Structural highlights ==
-[[3nyj]], [[3nyl]] – 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 />
-[[1z0q]], [[2beg]] – hAPP β-peptide – NMR<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
-===Amyloid precursor protein binary complex===
+==3D structures of amyloid precursor protein==
+[[Amyloid precursor protein 3D structures]]
-[[1ze9]] - hAPP zinc-binding domain + Zn – NMR<BR />
+</StructureSection>
-[[2fk1]], [[2fk2]], [[2fk3]], [[2fkl]] - hAPP residues 133-189 + Cu<BR />
-[[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 />
+== References ==
+<references/>
 [[Category:Topic Page]]