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Amyloid precursor protein

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{{STRUCTURE_3ktm| PDB=3ktm | SIZE=400| SCENE= |right| CAPTION=Human amyloid precursor protein E1-dimer domain complex with butane diol, sulfate and acetate, [[3ktm]] }}
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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]]'>
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'''Amyloid precursor protein''' (APP) is thought to regulate transcription. For detailed discussion see [[Human APP]] and [[Human APP Intracellular Domain Complex with Fe65-PTB2]].
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== Function ==
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{{TOC limit|limit=2}}
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'''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>
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==3D structures of amyloid precursor protein==
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== Disease ==
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''Update November 2011''
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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 />
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* [[Human APP]]<br />
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* [[Human APP Intracellular Domain Complex with Fe65-PTB2]]<br />
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* [[Beta Amyloid forms Plaques]]<br />
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* [[Amyloid beta]]
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[[3nyj]], [[3nyl]] – hAPP E2 domain – human<BR />
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== Structural highlights ==
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[[3ktm]] – hAPP residues 18-190<BR />
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[[1z0q]], [[2beg]] – hAPP β-peptide – NMR<BR />
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[[1ze7]], [[2bp4]] – hAPP zinc-binding domain – NMR<BR />
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[[2fjz]], [[2fma]] - hAPP residues 133-189<BR />
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[[1owt]] - hAPP residues 133-189 - NMR<BR />
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[[1rw6]] - hAPP residues 346-551<BR />
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[[1tkn]] - hAPP residues 460-569 - NMR<BR />
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[[1qyt]], [[1qwp]], [[1qxc]] - hAPP residues 25-35 – NMR<BR />
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[[1mwp]] - hAPP heparin-binding domain
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===Amyloid precursor protein binary complex===
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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.
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==3D structures of amyloid precursor protein==
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[[Amyloid precursor protein 3D structures]]
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[[1ze9]] - hAPP zinc-binding domain + Zn – NMR<BR />
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</StructureSection>
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[[2fk1]], [[2fk2]], [[2fk3]], [[2fkl]] - hAPP residues 133-189 + Cu<BR />
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[[3jti]], [[3gci]] – hAPP peptide + phospholipase A2<BR />
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[[3l81]] - hAPP peptide + AP-4 complex subunit μ-1<BR />
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[[3ifl]], [[3ifn]], [[3ifo]], [[3ifp]], [[2r0w]] - hAPP peptide + antibody<BR />
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[[2wk3]] - hAPP residues 1-42 + insulin degrading enzyme<BR />
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[[3dxc]] - hAPP residues 739-770 + Fe65-PTB2<BR />
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[[3dxd]], [[3dxe]] - hAPP residues 739-770 (mutant) + Fe65-PTB2<BR />
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[[2roz]] - hAPP peptide + Fe65 C terminal<BR />
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[[2otk]] - hAPP residues 672-711 + ZAB3 affibody dimer - NMR<BR />
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Human amyloid precursor protein heparin-binding domain 1mwp

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References

  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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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