View source for 6bxe


==Crystal structure of Variable Lymphocyte Receptor 9 (VLR9)==
<StructureSection load='6bxe' size='340' side='right'caption='[[6bxe]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6bxe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Petromyzon_marinus Petromyzon marinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BXE FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.651&#8491;</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=6bxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bxe OCA], [https://pdbe.org/6bxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bxe RCSB], [https://www.ebi.ac.uk/pdbsum/6bxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bxe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A5HBR7_PETMA A5HBR7_PETMA] 
<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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6bxe" style="background-color:#fffaf0;"></div>

==See Also==
*[[Variable lymphocyte receptor 3D structures|Variable lymphocyte receptor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Petromyzon marinus]]
[[Category: Cooper MD]]
[[Category: Gunn RJ]]
[[Category: Herrin BR]]
[[Category: Wilson IA]]