6cvj

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Current revision (14:30, 13 March 2024) (edit) (undo)
 
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<SX load='6cvj' size='340' side='right' viewer='molstar' caption='[[6cvj]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<SX load='6cvj' size='340' side='right' viewer='molstar' caption='[[6cvj]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6cvj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CVJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6CVJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6cvj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CVJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CVJ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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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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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6cvn|6cvn]]</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=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6cvj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cvj OCA], [http://pdbe.org/6cvj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cvj RCSB], [http://www.ebi.ac.uk/pdbsum/6cvj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cvj ProSAT]</span></td></tr>
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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=6cvj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cvj OCA], [https://pdbe.org/6cvj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cvj RCSB], [https://www.ebi.ac.uk/pdbsum/6cvj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cvj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/TBA1B_PIG TBA1B_PIG]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. [[http://www.uniprot.org/uniprot/TBB_PIG TBB_PIG]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.
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[https://www.uniprot.org/uniprot/TBA1B_PIG TBA1B_PIG] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Tau is a developmentally regulated axonal protein that stabilizes and bundles microtubules (MTs). Its hyperphosphorylation is thought to cause detachment from MTs and subsequent aggregation into fibrils implicated in Alzheimer's disease. It is unclear which tau residues are crucial for tau-MT interactions, where tau binds on MTs, and how it stabilizes them. We used cryo-electron microscopy to visualize different tau constructs on MTs, and computational approaches to generate atomic models of tau-tubulin interactions. The conserved tubulin-binding repeats within tau adopt similar extended structures along the crest of the protofilament, stabilizing the interface between tubulin dimers. Our structures explain the effect of phosphorylation on MT affinity and lead to a model of tau repeats binding in tandem along protofilaments, tethering together tubulin dimers and stabilizing polymerization interfaces.
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Near-atomic model of microtubule-tau interactions.,Kellogg EH, Hejab NMA, Poepsel S, Downing KH, DiMaio F, Nogales E Science. 2018 May 10. pii: science.aat1780. doi: 10.1126/science.aat1780. PMID:29748322<ref>PMID:29748322</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 6cvj" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Microtubule-associated protein 3D structures|Microtubule-associated protein 3D structures]]
*[[Microtubule-associated protein 3D structures|Microtubule-associated protein 3D structures]]
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*[[Tau protein|Tau protein]]
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*[[Tau protein 3D structures|Tau protein 3D structures]]
*[[Tubulin 3D Structures|Tubulin 3D Structures]]
*[[Tubulin 3D Structures|Tubulin 3D Structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</SX>
</SX>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Kellogg, E H]]
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[[Category: Kellogg EH]]
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[[Category: Nogales, E]]
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[[Category: Nogales E]]
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[[Category: Microtubule]]
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[[Category: Structural protein]]
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[[Category: Tau]]
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Current revision

Model of synthetic tau (four tandem repeats of first repeat sequence) bound to the microtubule

6cvj, resolution 3.20Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

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