2vq1: Difference between revisions
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<StructureSection load='2vq1' size='340' side='right'caption='[[2vq1]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2vq1' size='340' side='right'caption='[[2vq1]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2vq1]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2vq1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VQ1 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=2vq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vq1 OCA], [https://pdbe.org/2vq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vq1 RCSB], [https://www.ebi.ac.uk/pdbsum/2vq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vq1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Revision as of 14:43, 30 March 2022
anti trimeric Lewis X Fab54-5C10-Aanti trimeric Lewis X Fab54-5C10-A
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedLewis X trisaccharides normally function as essential cell-cell interaction mediators. However, oligomers of Lewis X trisaccharides expressed by the parasite Schistosoma mansoni seem to be related to its evasion of the immune response of its human host. Here we show that monoclonal antibody 54-5C10-A, which is used to diagnose schistosomiasis in humans, interacts with oligomers of at least three Lewis X trisaccharides, but not with monomeric Lewis X. We describe the sequence and the 2.5 A crystal structure of its Fab fragment and infer a possible mode of binding of the polymeric Lewis X from docking studies. Our studies indicate a radically different mode of binding compared to Fab 291-2G3-A, which is specific for monomeric Lewis X, thus providing a structural explanation of the diagnostic success of 54-5C10-A. Characterization of a diagnostic Fab fragment binding trimeric Lewis X.,de Geus DC, van Roon AM, Thomassen EA, Hokke CH, Deelder AM, Abrahams JP Proteins. 2009 Aug 1;76(2):439-47. PMID:19173313[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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