4hgw: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4hgw]] is a 2 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=4HGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HGW FirstGlance]. <br> | <table><tr><td colspan='2'>[[4hgw]] is a 2 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=4HGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HGW FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KDO:3-DEOXY-D-MANNO-OCT-2-ULOSONIC+ACID'>KDO</scene>, <scene name='pdbligand=KTU:PROP-2-EN-1-YL+3,5-DIDEOXY-ALPHA-D-THREO-OCT-5-EN-2-ULOPYRANOSIDONIC+ACID'>KTU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KDO:3-DEOXY-D-MANNO-OCT-2-ULOSONIC+ACID'>KDO</scene>, <scene name='pdbligand=KTU:PROP-2-EN-1-YL+3,5-DIDEOXY-ALPHA-D-THREO-OCT-5-EN-2-ULOPYRANOSIDONIC+ACID'>KTU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4hgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hgw OCA], [https://pdbe.org/4hgw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hgw RCSB], [https://www.ebi.ac.uk/pdbsum/4hgw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hgw ProSAT]</span></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=4hgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hgw OCA], [https://pdbe.org/4hgw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hgw RCSB], [https://www.ebi.ac.uk/pdbsum/4hgw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hgw ProSAT]</span></td></tr> | ||
</table> | </table> |
Latest revision as of 18:05, 20 September 2023
Crystal structure of S25-2 in complex with a 5,6-dehydro-Kdo disaccharideCrystal structure of S25-2 in complex with a 5,6-dehydro-Kdo disaccharide
Structural highlights
Publication Abstract from PubMedThe near-germline antibody S25-2 exhibits a remarkable cross-reactivity for oligosaccharides containing the bacterial lipopolysaccharide carbohydrate 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo). The recent synthesis of a variety of Kdo analogues permits a detailed structural analysis of the importance of specific interactions in antigen recognition by S25-2. The Kdo disaccharide analogue Kdo-(2-->4)-5,6-dehydro-Kdo lacks a 5-OH group on the second Kdo residue and has been cocrystallized with S25-2. The structure reveals that the modification of the Kdo residue at position 5 results in a rearrangement of intramolecular hydrogen bonds in the antigen that allows it to assume a novel conformation in the antibody-combining site. The cross-reactive binding of S25-2 to this synthetic ligand highlights the adaptability of this antibody to non-natural synthetic analogues. Exploring the cross-reactivity of S25-2: complex with a 5,6-dehydro-Kdo disaccharide.,Brooks CL, Wimmer K, Kosma P, Muller-Loennies S, Brade L, Brade H, Evans SV Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jan 1;69(Pt 1):2-5. doi:, 10.1107/S1744309112047422. Epub 2012 Dec 25. PMID:23295476[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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