Amyloid precursor protein

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
{{STRUCTURE_1mwp| PDB=1mwp | SIZE=400| SCENE= |right| CAPTION=Human amyloid precursor protein heparin-binding domain [[1mwp]] }}
+
{{STRUCTURE_1mwp| PDB=1mwp | SIZE=400| SCENE= |right| 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 ==
 +
 
 +
'''Amyloid precursor protein''' (APP) is a transmembranal protein which is thought to regulate transcription. APP plays a role in synaptic formation and repair.
 +
 
 +
== 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]]<br />
* [[Human APP Intracellular Domain Complex with Fe65-PTB2]]<br />
* [[Human APP Intracellular Domain Complex with Fe65-PTB2]]<br />
* [[Amyloid beta]].
* [[Amyloid beta]].
-
__NOTOC__
+
== Structural highlights ==
 +
 
 +
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.
==3D structures of amyloid precursor protein==
==3D structures of amyloid precursor protein==
Line 22: Line 30:
**[[1rw6]] - hAPP residues 346-551<BR />
**[[1rw6]] - hAPP residues 346-551<BR />
**[[1tkn]] - hAPP residues 460-569 - NMR<BR />
**[[1tkn]] - hAPP residues 460-569 - NMR<BR />
-
**[[1qyt]], [[1qwp]], [[1qxc]] - hAPP residues 25-35 – NMR<BR />
 
**[[1mwp]] - hAPP heparin-binding domain<br />
**[[1mwp]] - hAPP heparin-binding domain<br />
Line 29: Line 36:
**[[1z0q]], [[2beg]] – hAPP β-peptide residues 1-42 – NMR<br />
**[[1z0q]], [[2beg]] – hAPP β-peptide residues 1-42 – NMR<br />
**[[1amb]], [[1amc]] – hAPP β-peptide residues 1-28 – NMR<br />
**[[1amb]], [[1amc]] – hAPP β-peptide residues 1-28 – NMR<br />
-
**[[1qcm]], [[1qwp]], [[1qxc]], [[1qyt]] – hAPP β-peptide residues 25-35 – NMR<br />
+
**[[1qcm]], [[1qyt]], [[1qwp]], [[1qxc]] – hAPP β-peptide residues 25-35 – NMR<br />
**[[1ba4]], [[1ba6]], [[2lnq]] – hAPP β-peptide residues 1-40 – NMR<br />
**[[1ba4]], [[1ba6]], [[2lnq]] – hAPP β-peptide residues 1-40 – NMR<br />
**[[1bjb]], [[1bjc]] – hAPP β-peptide residues 1-28 (mutant) – NMR<br />
**[[1bjb]], [[1bjc]] – hAPP β-peptide residues 1-28 (mutant) – NMR<br />
Line 42: Line 49:
**[[1ze9]] - hAPP zinc-binding domain + Zn – NMR<BR />
**[[1ze9]] - hAPP zinc-binding domain + Zn – NMR<BR />
**[[2fk1]], [[2fk2]], [[2fk3]], [[2fkl]] - hAPP residues 133-189 + Cu<BR />
**[[2fk1]], [[2fk2]], [[2fk3]], [[2fkl]] - hAPP residues 133-189 + Cu<BR />
-
**[[3jti]], [[3gci]] – hAPP peptide + phospholipase A2<BR />
+
**[[3jti]], [[3gci]] – hAPP peptide residues 699-706 + phospholipase A2<BR />
-
**[[3l81]] - hAPP peptide + AP-4 complex subunit μ-1<BR />
+
**[[3l81]] - hAPP peptide residues 761-767 + AP-4 complex subunit μ-1<BR />
-
**[[3ifl]], [[3ifn]], [[3ifo]], [[3ifp]], [[2r0w]] - hAPP peptide + antibody<BR />
+
**[[3ifl]], [[3ifn]], [[3ifo]], [[3ifp]], [[2r0w]] - hAPP peptide residues 672-711 + antibody<BR />
-
**[[2wk3]] - hAPP residues 1-42 + insulin degrading enzyme<BR />
+
**[[2wk3]] - hAPP residues 672-713 + insulin degrading enzyme<BR />
**[[3dxc]] - hAPP residues 739-770 + Fe65-PTB2<BR />
**[[3dxc]] - hAPP residues 739-770 + Fe65-PTB2<BR />
**[[3dxd]], [[3dxe]] - hAPP residues 739-770 (mutant) + Fe65-PTB2<BR />
**[[3dxd]], [[3dxe]] - hAPP residues 739-770 (mutant) + Fe65-PTB2<BR />
-
**[[2roz]] - hAPP peptide + Fe65 C terminal<BR />
+
**[[2roz]] - hAPP peptide residues 582-704 + Fe65 C terminal<BR />
**[[2otk]] - hAPP residues 672-711 + ZAB3 affibody dimer - NMR<BR />
**[[2otk]] - hAPP residues 672-711 + ZAB3 affibody dimer - NMR<BR />
**[[3l3t]] - hAPP residues 211-267 + mesotrypsin<br />
**[[3l3t]] - hAPP residues 211-267 + mesotrypsin<br />

Revision as of 11:04, 1 November 2015

PDB ID 1mwp

Drag the structure with the mouse to rotate
Human amyloid precursor protein heparin-binding domain 1mwp
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Contents

Function

Amyloid precursor protein (APP) is a transmembranal protein which is thought to regulate transcription. APP plays a role in synaptic formation and repair.

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

Structural highlights

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.

3D structures of amyloid precursor protein

Updated on 01-November-2015

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

Retrieved from "http://52.214.119.220/wiki/index.php/Amyloid_precursor_protein"
Personal tools