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Amyloid precursor protein
From Proteopedia
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| - | {{ | + | {{STRUCTURE_1mwp| PDB=1mwp | SIZE=400| SCENE= |right| CAPTION=Human amyloid precursor protein E1-dimer domain complex with butane diol, sulfate and acetate, [[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]]. | '''Amyloid precursor protein''' (APP) is thought to regulate transcription. For detailed discussion see [[Human APP]] and [[Human APP Intracellular Domain Complex with Fe65-PTB2]]. | ||
Revision as of 11:00, 11 December 2012
Amyloid precursor protein (APP) is thought to regulate transcription. For detailed discussion see Human APP and Human APP Intracellular Domain Complex with Fe65-PTB2.
3D structures of amyloid precursor protein
Update May 2012
3nyj, 3nyl, 3umh, 3umi, 3umk – hAPP E2 domain – human
3ktm – hAPP residues 18-190
1z0q, 2beg – hAPP β-peptide – NMR
1ze7, 2bp4 – hAPP zinc-binding domain – NMR
2fjz, 2fma - hAPP residues 133-189
1owt - hAPP residues 133-189 - NMR
1rw6 - hAPP residues 346-551
1tkn - hAPP residues 460-569 - NMR
1qyt, 1qwp, 1qxc - hAPP residues 25-35 – NMR
1mwp - hAPP heparin-binding domain
Amyloid precursor protein binary complex
1ze9 - hAPP zinc-binding domain + Zn – NMR
2fk1, 2fk2, 2fk3, 2fkl - hAPP residues 133-189 + Cu
3jti, 3gci – hAPP peptide + phospholipase A2
3l81 - hAPP peptide + AP-4 complex subunit μ-1
3ifl, 3ifn, 3ifo, 3ifp, 2r0w - hAPP peptide + antibody
2wk3 - hAPP residues 1-42 + insulin degrading enzyme
3dxc - hAPP residues 739-770 + Fe65-PTB2
3dxd, 3dxe - hAPP residues 739-770 (mutant) + Fe65-PTB2
2roz - hAPP peptide + Fe65 C terminal
2otk - hAPP residues 672-711 + ZAB3 affibody dimer - NMR
3l3t - hAPP residues 211-267 + mesotrypsin
3l33 - hAPP residues 290-341 + trypsin-3 (mutant)


