9fh1

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Current revision (09:38, 22 October 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9fh1 is ON HOLD until Paper Publication
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==Cryo-EM Structure of Amyloid-beta Fibrils from Mouse Brain Carrying the Uppsala AbetaUpp(1-42)delta(19-24) Mutation==
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<StructureSection load='9fh1' size='340' side='right'caption='[[9fh1]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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Authors: Zielinski, M., Peralta Reyes, F.S., Gremer, L., Pagnon de la Vega, M., Roeder, C., Heidler, T.V., Syvaenen, S., Willbold, D., Sehlin, D., Ingelsson, M., Schroeder, G.F.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9fh1]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9FH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9FH1 FirstGlance]. <br>
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Description: Cryo-EM Structure of Amyloid-beta Fibrils from Mouse Brain Carrying the Uppsala AbetaUpp(1-42)delta(19-24) Mutation
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9fh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9fh1 OCA], [https://pdbe.org/9fh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9fh1 RCSB], [https://www.ebi.ac.uk/pdbsum/9fh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9fh1 ProSAT]</span></td></tr>
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[[Category: Syvaenen, S]]
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</table>
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[[Category: Willbold, D]]
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== Function ==
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[[Category: Schroeder, G.F]]
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[https://www.uniprot.org/uniprot/A4_CANLF A4_CANLF] Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP (By similarity). Inhibits G(o)-alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapses in axons (By similarity). May be involved in copper homeostasis/oxidative stress through copper ion reduction (By similarity). In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation (By similarity). Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1 (By similarity).[UniProtKB:P05067]
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[[Category: Ingelsson, M]]
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__TOC__
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[[Category: Pagnon De La Vega, M]]
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</StructureSection>
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[[Category: Heidler, T.V]]
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[[Category: Large Structures]]
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[[Category: Gremer, L]]
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[[Category: Mus musculus]]
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[[Category: Sehlin, D]]
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[[Category: Gremer L]]
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[[Category: Zielinski, M]]
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[[Category: Heidler TV]]
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[[Category: Roeder, C]]
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[[Category: Ingelsson M]]
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[[Category: Peralta Reyes, F.S]]
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[[Category: Pagnon de la Vega M]]
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[[Category: Peralta Reyes FS]]
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[[Category: Roeder C]]
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[[Category: Schroeder GF]]
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[[Category: Sehlin D]]
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[[Category: Syvaenen S]]
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[[Category: Willbold D]]
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[[Category: Zielinski M]]

Current revision

Cryo-EM Structure of Amyloid-beta Fibrils from Mouse Brain Carrying the Uppsala AbetaUpp(1-42)delta(19-24) Mutation

PDB ID 9fh1

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