5uf4: Difference between revisions
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<StructureSection load='5uf4' size='340' side='right'caption='[[5uf4]], [[Resolution|resolution]] 2.04Å' scene=''> | <StructureSection load='5uf4' size='340' side='right'caption='[[5uf4]], [[Resolution|resolution]] 2.04Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5uf4]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5uf4]] is a 3 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=5UF4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UF4 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.04Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5uf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uf4 OCA], [https://pdbe.org/5uf4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uf4 RCSB], [https://www.ebi.ac.uk/pdbsum/5uf4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uf4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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==See Also== | ==See Also== | ||
*[[Variable lymphocyte receptor|Variable lymphocyte receptor]] | *[[Variable lymphocyte receptor 3D structures|Variable lymphocyte receptor 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Petromyzon marinus]] | ||
[[Category: Collins | [[Category: Collins BC]] | ||
[[Category: Cooper | [[Category: Cooper MD]] | ||
[[Category: Cummings | [[Category: Cummings RD]] | ||
[[Category: Gunn | [[Category: Gunn RJ]] | ||
[[Category: Herrin | [[Category: Herrin BR]] | ||
[[Category: McKitrick | [[Category: McKitrick TR]] | ||
[[Category: Wilson | [[Category: Wilson IA]] | ||
Latest revision as of 16:26, 4 October 2023
Crystal Structure of Variable Lymphocyte Receptor (VLR) O13 with LNnT boundCrystal Structure of Variable Lymphocyte Receptor (VLR) O13 with LNnT bound
Structural highlights
Publication Abstract from PubMedHigh-quality reagents to study and detect glycans with high specificity for research and clinical applications are severely lacking. Here, we structurally and functionally characterize several variable lymphocyte receptor (VLR)-based antibodies from lampreys immunized with O erythrocytes that specifically recognize the blood group H-trisaccharide type II antigen. Glycan microarray analysis and biophysical data reveal that these VLRs exhibit greater specificity for H-trisaccharide compared with the plant lectin UEA-1, which is widely used in blood typing. Among these antibodies, O13 exhibits superior specificity for H-trisaccharide, the basis for which is revealed by comparative analysis of high-resolution VLR:glycan crystal structures. Using a structure-guided approach, we designed an O13 mutant with further enhanced specificity for H-trisaccharide. These insights into glycan recognition by VLRs suggest that lampreys can produce highly specific glycan antibodies, and are a valuable resource for the production of next-generation glycan reagents for biological and biomedical research and as diagnostics and therapeutics. Structural Insights into VLR Fine Specificity for Blood Group Carbohydrates.,Collins BC, Gunn RJ, McKitrick TR, Cummings RD, Cooper MD, Herrin BR, Wilson IA Structure. 2017 Sep 27. pii: S0969-2126(17)30294-0. doi:, 10.1016/j.str.2017.09.003. PMID:28988747[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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