Human APP Intracellular Domain Complex with Fe65-PTB2: Difference between revisions
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{{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. | |||
== 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. | ||