|
|
(10 intermediate revisions by 2 users not shown) |
Line 1: |
Line 1: |
| {{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]] |