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6fay
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Teneurin3 monomer== | |
| + | <StructureSection load='6fay' size='340' side='right' caption='[[6fay]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6fay]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FAY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FAY FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6fay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fay OCA], [http://pdbe.org/6fay PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fay RCSB], [http://www.ebi.ac.uk/pdbsum/6fay PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fay ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Teneurins are ancient cell-cell adhesion receptors that are vital for brain development and synapse organisation. They originated in early metazoan evolution through a horizontal gene transfer event when a bacterial YD-repeat toxin fused to a eukaryotic receptor. We present X-ray crystallography and cryo-EM structures of two Teneurins, revealing a ~200 kDa extracellular super-fold in which eight sub-domains form an intricate structure centred on a spiralling YD-repeat shell. An alternatively spliced loop, which is implicated in homophilic Teneurin interaction and specificity, is exposed and thus poised for interaction. The N-terminal side of the shell is 'plugged' via a fibronectin-plug domain combination, which defines a new class of YD proteins. Unexpectedly, we find that these proteins are widespread amongst modern bacteria, suggesting early metazoan receptor evolution from a distinct class of proteins, which today includes both bacterial proteins and eukaryotic Teneurins. | ||
| - | + | Structures of Teneurin adhesion receptors reveal an ancient fold for cell-cell interaction.,Jackson VA, Meijer DH, Carrasquero M, van Bezouwen LS, Lowe ED, Kleanthous C, Janssen BJC, Seiradake E Nat Commun. 2018 Mar 14;9(1):1079. doi: 10.1038/s41467-018-03460-0. PMID:29540701<ref>PMID:29540701</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6fay" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bezouwen, L S.van]] | ||
| + | [[Category: Janssen, B J.C]] | ||
| + | [[Category: Meijer, D H.M]] | ||
| + | [[Category: Bacterial toxin-like]] | ||
| + | [[Category: Cell adhesion]] | ||
| + | [[Category: Neuronal cell adhesion]] | ||
Revision as of 06:41, 28 March 2018
Teneurin3 monomer
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