Amyloid precursor protein

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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.
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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</StructureSection>
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==3D structures of amyloid precursor protein==
==3D structures of amyloid precursor protein==
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[[Amyloid precursor protein 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*APP
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**[[3nyj]], [[3nyl]], [[3umh]], [[3umi]], [[3umk]] – hAPP E2 domain – human<BR />
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**[[4pwq]], [[3ktm]] - hAPP E1 domain<br />
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**[[3ktm]] – hAPP residues 18-190<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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**[[5buo]] – hAPP residues 351-691<br />
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**[[1tkn]] - hAPP residues 460-569 - NMR<BR />
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**[[1mwp]], [[4pqd]] - hAPP heparin-binding domain<br />
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**[[5txd]] – hAPP residues 698-703<br />
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**[[5how]], [[5hox]], [[5hoy]] – hAPP residues 698-707 (mutant)<br />
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**[[5aef]] – hAPP residues 630-657 – Cryo EM<br />
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*hAPP β-peptide
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**[[1z0q]], [[2beg]] – hAPP β-peptide residues 1-42 – NMR<br />
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**[[5oqv]] – hAPP -peptide residues 1-42 – Cryo EM<br />
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**[[1amb]], [[1amc]] – hAPP β-peptide residues 1-28 – NMR<br />
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**[[1qcm]], [[1qyt]], [[1qwp]], [[1qxc]] – hAPP β-peptide residues 25-35 – NMR<br />
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**[[1ba4]], [[1ba6]], [[2lnq]] – hAPP β-peptide residues 1-40 – NMR<br />
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**[[1bjb]], [[1bjc]] – hAPP β-peptide residues 1-28 (mutant) – NMR<br />
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**[[5lfy]] – hAPP -peptide residues 17-26 – NMR<br />
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**[[1nmj]] – APP β-peptide residues 1-28 – rat – NMR<br />
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**[[3bae]] – hAPP β-peptide residues 1-28 + antibody<br />
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**[[3bkj]] – hAPP β-peptide residues 1-16 + antibody<br />
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**[[2roz]] – hAPP β-peptide residues 1-32 + amyloid β A4 precursor protein - NMR<br />
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**[[2wk3]] – hAPP β-peptide residues 1-42 + insulin-degrading enzyme<br />
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*Amyloid precursor protein binary complex
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**[[1ze9]] - hAPP zinc-binding domain + Zn – NMR<BR />
 
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**[[2fk1]], [[2fk2]], [[2fk3]], [[2fkl]] - hAPP residues 133-189 + Cu<BR />
 
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**[[3jti]], [[3gci]] – hAPP peptide residues 699-706 + phospholipase A2<BR />
 
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**[[3l81]] - hAPP peptide residues 761-767 + AP-4 complex subunit μ-1<BR />
 
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**[[3ifl]], [[3ifn]], [[3ifo]], [[3ifp]], [[2r0w]] - hAPP peptide residues 672-711 + antibody<BR />
 
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**[[2wk3]] - hAPP residues 672-713 + 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 residues 582-704 + Fe65 C terminal<BR />
 
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**[[2otk]] - hAPP residues 672-711 + ZAB3 affibody dimer - NMR<BR />
 
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**[[3l3t]] - hAPP residues 211-267 + mesotrypsin<br />
 
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**[[3l33]], [[5c67]] - hAPP residues 290-341 + trypsin-3 (mutant)<br />
 
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**[[5amb]] – hAPP residues 706-713 + angiotensin-converting enzyme<br />
 
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**[[5am8]] – hAPP residues 675-681 + angiotensin-converting enzyme<br />
 
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}}
 
== References ==
== References ==
<references/>
<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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