Human APP Intracellular Domain Complex with Fe65-PTB2: Difference between revisions

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'''Intracellular domain of human APP in complex with Fe65-PTB2'''
{{STRUCTURE_3dxc |  PDB=3dxc | SIZE=400| SCENE= |right|  CAPTION=Human amyloid precursor protein residues 739-770 complex with Fe65-PTB2, [[3dxc]]    }}Cleavage of the '''amyloid precursor protein''' (APP) is a crucial event in Alzheimer disease pathogenesis that creates the amyloid-beta peptide (Abeta) and liberates the carboxy-terminal APP intracellular domain (AICD) into the cytosol. <ref>PMID:18833287</ref> The study of interaction of the AICD and Fe65 protein is rather important, as Fe65 protein seems to be implicated in production of Abeta and in signalling in APP.
 
Cleavage of the amyloid precursor protein (APP) is a crucial event in Alzheimer disease pathogenesis that creates the amyloid-beta peptide (Abeta) and liberates the carboxy-terminal APP intracellular domain (AICD) into the cytosol. <ref>PMID:18833287</ref> The study of interaction of the AICD and Fe65 protein is rather important, as Fe65 protein seems to be implicated in production of Abeta and in signalling in APP.
{{STRUCTURE_3dxc |  PDB=3dxc  |  SCENE=  }}


== Structure ==
== Structure ==
This crystal structure contains 4 chains. <scene name='SANDBOX138/Chainesaandc/1'>A chain is identical to C chain</scene>. Each contains 140 residues: 4 helices and 7 strands. It's a part of the protein Fe65 binded with APP intracellular domain.
This crystal structure contains 4 chains. <scene name='SANDBOX138/Chainesaandc/1'>A chain is identical to C chain</scene>. Each contains 140 residues: 4 helices and 7 strands. It's a part of the protein Fe65 binded with APP intracellular domain.
<scene name='SANDBOX138/Chains_bandd/2'>Chains B and D are also identical</scene>. Each contains 35 residues: 2 helices and 1 strand. They represent APP intracellular domain.
<scene name='SANDBOX138/Chains_bandd/2'>Chains B and D are also identical</scene>. Each contains 35 residues: 2 helices and 1 strand. They represent APP intracellular domain.
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Besides neuritic plaques neurofibrillary tangles containing hyperphosphorylated tau protein are characteristic in the neuropathology of Alzheimer’s disease. Hyperphosphorylated tau protein and accumulated Aβ protein are considered to coexist. <ref>PMID: 19158417</ref>
Besides neuritic plaques neurofibrillary tangles containing hyperphosphorylated tau protein are characteristic in the neuropathology of Alzheimer’s disease. Hyperphosphorylated tau protein and accumulated Aβ protein are considered to coexist. <ref>PMID: 19158417</ref>
==3D structures of amyloid precursor protein==
[[Amyloid precursor protein]]
===Additional Resources===
For additional information, see: [[Alzheimer's Disease]]
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== References ==
== References ==
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