5ufb: Difference between revisions

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'''Unreleased structure'''


The entry 5ufb is ON HOLD  until Paper Publication
==Crystal Structure of Variable Lymphocyte Receptor (VLR) Tn4-22 (Apo)==
<StructureSection load='5ufb' size='340' side='right' caption='[[5ufb]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ufb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UFB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UFB FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uei|5uei]], [[5uf1|5uf1]], [[5uf4|5uf4]], [[5ufc|5ufc]], [[5ufd|5ufd]], [[5uff|5uff]]</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=5ufb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ufb OCA], [http://pdbe.org/5ufb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ufb RCSB], [http://www.ebi.ac.uk/pdbsum/5ufb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ufb ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
High-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.


Authors:  
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<ref>PMID:28988747</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 5ufb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Collins, B C]]
[[Category: Cooper, M D]]
[[Category: Cummings, R D]]
[[Category: Gunn, R J]]
[[Category: Herrin, B R]]
[[Category: McKitrick, T R]]
[[Category: Wilson, I A]]
[[Category: Adaptive immunity]]
[[Category: Glycan binding]]
[[Category: Glycan receptor]]
[[Category: Immune system]]
[[Category: Jawless fish]]
[[Category: Leucine-rich repeat]]
[[Category: Lrr]]
[[Category: Receptor]]
[[Category: Sea lamprey]]
[[Category: Variable lymphocyte receptor]]
[[Category: Vlr]]

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