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

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<scene name='SANDBOX138/Chains_bandd/1'>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/1'>Chains B and D are also identical</scene>. Each contains 35 residues: 2 helices and 1 strand. They represent APP intracellular domain.


The crystal structure of the APP intracellular domain is in complex with the <scene name='SANDBOX138/Ptb/1'>C-terminal phosphotyrosine-binding (PTB) domain of Fe65</scene>.  The interaction of the APP C terminus with the adaptor protein Fe65 mediates APP trafficking and signalling, and is thought to regulate APP processing and Abeta generation. The unique interface involves the NPxY PTB-binding motif and two alpha helices. The amino-terminal helix of the APP intracellular domain is
The APP intracellular domain is in complex with the <scene name='SANDBOX138/Ptb/1'>C-terminal phosphotyrosine-binding (PTB) domain of Fe65</scene>.  The interaction of the APP C terminus with the adaptor protein Fe65 mediates APP trafficking and signalling, and is thought to regulate APP processing and Abeta generation. The unique interface involves the NPxY PTB-binding motif and two alpha helices. The amino-terminal helix of the APP intracellular domain is
<scene name='SANDBOX138/T668/2'>capped by threonine T(668)</scene>, it's an Alzheimer disease-relevant phosphorylation site which is involved in Fe65-binding regulation. The structure together with mutational studies, isothermal titration calorimetry and nuclear magnetic resonance experiments sets the stage for understanding T(668) phosphorylation-dependent complex regulation at a molecular level.<ref>PMID:18833287</ref> Mutation at Thr-668 of APP abolished the effect of Fe65 on APP maturation. This mutation blocked the Fe65-dependent suppression of Abeta production and resulted in the release of increased levels of Abeta in the presence of Fe65 <ref>PMID:11517218</ref> .
<scene name='SANDBOX138/T668/2'>capped by threonine T(668)</scene>, it's an Alzheimer disease-relevant phosphorylation site which is involved in Fe65-binding regulation. The structure together with mutational studies, isothermal titration calorimetry and nuclear magnetic resonance experiments sets the stage for understanding T(668) phosphorylation-dependent complex regulation at a molecular level.<ref>PMID:18833287</ref> Mutation at Thr-668 of APP abolished the effect of Fe65 on APP maturation. This mutation blocked the Fe65-dependent suppression of Abeta production and resulted in the release of increased levels of Abeta in the presence of Fe65 <ref>PMID:11517218</ref> .


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