8ohi

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Current revision (14:45, 6 November 2024) (edit) (undo)
 
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<StructureSection load='8ohi' size='340' side='right'caption='[[8ohi]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='8ohi' size='340' side='right'caption='[[8ohi]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[8ohi]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8OHI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8OHI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[8ohi]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8OHI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8OHI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HIA:L-HISTIDINE+AMIDE'>HIA</scene>, <scene name='pdbligand=VP1:Fluorenylmethyloxycarbonyl+chloride'>VP1</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=VP1:9~{H}-fluoren-9-ylmethyl+carbonochloridate'>VP1</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8ohi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ohi OCA], [https://pdbe.org/8ohi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ohi RCSB], [https://www.ebi.ac.uk/pdbsum/8ohi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ohi ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8ohi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ohi OCA], [https://pdbe.org/8ohi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ohi RCSB], [https://www.ebi.ac.uk/pdbsum/8ohi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ohi ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/TAU_HUMAN TAU_HUMAN] Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization.<ref>PMID:21985311</ref>
[https://www.uniprot.org/uniprot/TAU_HUMAN TAU_HUMAN] Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization.<ref>PMID:21985311</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Tauopathies encompass a group of neurodegenerative disorders characterised by diverse tau amyloid fibril structures. The persistence of polymorphism across tauopathies suggests that distinct pathological conditions dictate the adopted polymorph for each disease. However, the extent to which intrinsic structural tendencies of tau amyloid cores contribute to fibril polymorphism remains uncertain. Using a combination of experimental approaches, we here identify a new amyloidogenic motif, PAM4 (Polymorphic Amyloid Motif of Repeat 4), as a significant contributor to tau polymorphism. Calculation of per-residue contributions to the stability of the fibril cores of different pathologic tau structures suggests that PAM4 plays a central role in preserving structural integrity across amyloid polymorphs. Consistent with this, cryo-EM structural analysis of fibrils formed from a synthetic PAM4 peptide shows that the sequence adopts alternative structures that closely correspond to distinct disease-associated tau strains. Furthermore, in-cell experiments revealed that PAM4 deletion hampers the cellular seeding efficiency of tau aggregates extracted from Alzheimer's disease, corticobasal degeneration, and progressive supranuclear palsy patients, underscoring PAM4's pivotal role in these tauopathies. Together, our results highlight the importance of the intrinsic structural propensity of amyloid core segments to determine the structure of tau in cells, and in propagating amyloid structures in disease.
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Local structural preferences in shaping tau amyloid polymorphism.,Louros N, Wilkinson M, Tsaka G, Ramakers M, Morelli C, Garcia T, Gallardo R, D'Haeyer S, Goossens V, Audenaert D, Thal DR, Mackenzie IR, Rademakers R, Ranson NA, Radford SE, Rousseau F, Schymkowitz J Nat Commun. 2024 Feb 3;15(1):1028. doi: 10.1038/s41467-024-45429-2. PMID:38310108<ref>PMID:38310108</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8ohi" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Synthetic construct]]
 
[[Category: Audenaert D]]
[[Category: Audenaert D]]
[[Category: D'Haeyer S]]
[[Category: D'Haeyer S]]

Current revision

Structure of the Fmoc-Tau-PAM4 Type 2 amyloid fibril

PDB ID 8ohi

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