4hgw: Difference between revisions
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[[ | ==Crystal structure of S25-2 in complex with a 5,6-dehydro-Kdo disaccharide== | ||
<StructureSection load='4hgw' size='340' side='right' caption='[[4hgw]], [[Resolution|resolution]] 1.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4hgw]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HGW FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <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></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=4hgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hgw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hgw RCSB], [http://www.ebi.ac.uk/pdbsum/4hgw PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The 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<ref>PMID:23295476</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Antibody|Antibody]] | |||
== | == References == | ||
[[ | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Brooks, C L | [[Category: Brooks, C L]] | ||
[[Category: Evans, S V | [[Category: Evans, S V]] | ||
[[Category: Antibody]] | [[Category: Antibody]] | ||
[[Category: Immune system]] | [[Category: Immune system]] | ||
[[Category: Lp]] | [[Category: Lp]] |
Revision as of 12:40, 10 December 2014
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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