6bxa: Difference between revisions

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-'''Unreleased structure'''
-The entry 6bxa is ON HOLD  until Paper Publication
+==Crystal structure of N-terminal fragment of Zebrafish Toll-Like Receptor 5 (TLR5) with Lamprey Variable Lymphocyte Receptor 2 (VLR2) bound==
+<StructureSection load='6bxa' size='340' side='right' caption='[[6bxa]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6bxa]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BXA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BXA FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <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=6bxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bxa OCA], [http://pdbe.org/6bxa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bxa RCSB], [http://www.ebi.ac.uk/pdbsum/6bxa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bxa ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Variable lymphocyte receptors (VLRs) are unconventional adaptive immune receptors relatively recently discovered in the phylogenetically ancient jawless vertebrates, lamprey and hagfish. VLRs bind antigens using a leucine-rich repeat fold and are the only known adaptive immune receptors that do not utilize an immunoglobulin fold for antigen recognition. While immunoglobulin antibodies have been studied extensively, there are comparatively few studies on antigen recognition by VLRs, particularly for protein antigens. Here we report isolation, functional and structural characterization of three VLRs that bind the protein toll-like receptor 5 (TLR5) from zebrafish. Two of the VLRs block binding of TLR5 to its cognate ligand flagellin in functional assays using reporter cells. Co-crystal structures revealed that these VLRs bind to two different epitopes on TLR5, both of which include regions involved in flagellin binding. Our work here demonstrates that the lamprey adaptive immune system can be used to generate high-affinity VLR clones that recognize different epitopes and differentially impact natural ligand binding to a protein antigen.
-Authors:
+VLR Recognition of TLR5 Expands the Molecular Characterization of Protein Antigen Binding by Non-Ig-based Antibodies.,Gunn RJ, Herrin BR, Acharya S, Cooper MD, Wilson IA J Mol Biol. 2018 Apr 27;430(9):1350-1367. doi: 10.1016/j.jmb.2018.03.016. Epub, 2018 Mar 26. PMID:29596914<ref>PMID:29596914</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6bxa" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Cooper, M D]]
+[[Category: Gunn, R J]]
+[[Category: Herrin, B R]]
+[[Category: Wilson, I A]]
+[[Category: Antibody]]
+[[Category: Immune system]]
+[[Category: Leucine-rich repeat]]
+[[Category: Vlr]]