View source for 4k79


==Recognition of the Thomsen-Friedenreich Antigen by a Lamprey Variable Lymphocyte Receptor==
<StructureSection load='4k79' size='340' side='right'caption='[[4k79]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4k79]] is a 4 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=4K79 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K79 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</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=4k79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k79 OCA], [https://pdbe.org/4k79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k79 RCSB], [https://www.ebi.ac.uk/pdbsum/4k79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k79 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/K0IE77_PETMA K0IE77_PETMA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Variable lymphocyte receptors (VLRs) are leucine-rich repeat (LRR) proteins that mediate adaptive immunity in jawless vertebrates. VLRs were recently shown to recognize glycans, such as the tumor-associated Thomsen-Friedenreich antigen (TFalpha; Galbeta1-3GalNAcalpha), with a selectivity rivaling or exceeding that of lectins and antibodies. To understand the basis for TFalpha recognition by one such VLR (VLRB.aGPA.23), we measured thermodynamic parameters for the binding interaction, and determined the structure of the VLRB.aGPA.23-TFalpha complex to 2.2 A resolution. In the structure, four tryptophan residues form a tight hydrophobic cage encasing the TFalpha disaccharide that completely excludes buried water molecules. This cage, together with hydrogen bonding of sugar hydroxyls to polar side chains, explains the high selectivity of VLRB.aGPA.23. The topology of the glycan-binding site of VLRB.aGPA.23 differs markedly from those of lectins or antibodies, which typically consist of long, convex grooves for accommodating the oligosaccharide. Instead, the TFalpha disaccharide is sandwiched between a variable loop and the concave surface of the VLR formed by the beta-strands of the LRR modules. Longer oligosaccharides are predicted to extend perpendicularly across the beta-strands, requiring them to bend to match the concavity of the VLR solenoid.

Recognition of the Thomsen-Friedenreich pancarcinoma carbohydrate antigen by a lamprey variable lymphocyte receptor.,Luo M, Velikovsky CA, Yang X, Siddiqui MA, Hong X, Barchi JJ, Gildersleeve JC, Pancer Z, Mariuzza RA J Biol Chem. 2013 Jun 19. PMID:23782692<ref>PMID:23782692</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4k79" 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: Luo M]]
[[Category: Mariuzza RA]]
[[Category: Velikovsky CA]]
[[Category: Yang XB]]