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| | <StructureSection load='4hxb' size='340' side='right'caption='[[4hxb]], [[Resolution|resolution]] 2.45Å' scene=''> | | <StructureSection load='4hxb' size='340' side='right'caption='[[4hxb]], [[Resolution|resolution]] 2.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4hxb]] 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=4HXB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HXB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4hxb]] 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=4HXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HXB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hxa|4hxa]]</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=4hxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hxb OCA], [https://pdbe.org/4hxb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hxb RCSB], [https://www.ebi.ac.uk/pdbsum/4hxb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hxb ProSAT]</span></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=4hxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hxb OCA], [http://pdbe.org/4hxb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hxb RCSB], [http://www.ebi.ac.uk/pdbsum/4hxb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hxb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
| - | [[Category: Brisson, J R]] | + | [[Category: Brisson JR]] |
| - | [[Category: Evans, S V]] | + | [[Category: Evans SV]] |
| - | [[Category: Jachymek, W]] | + | [[Category: Jachymek W]] |
| - | [[Category: Jarrell, H C]] | + | [[Category: Jarrell HC]] |
| - | [[Category: Jennings, H J]] | + | [[Category: Jennings HJ]] |
| - | [[Category: Johal, A R]] | + | [[Category: Johal AR]] |
| - | [[Category: Khieu, N H]] | + | [[Category: Khieu NH]] |
| - | [[Category: Landry, R C]] | + | [[Category: Landry RC]] |
| - | [[Category: Letts, J A]] | + | [[Category: Letts JA]] |
| - | [[Category: Yang, Q]] | + | [[Category: Yang Q]] |
| - | [[Category: Antibody]]
| + | |
| - | [[Category: Carbohydrate-binding]]
| + | |
| - | [[Category: Complementarity determining region]]
| + | |
| - | [[Category: Fab]]
| + | |
| - | [[Category: Immune system]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Monoclonal antibodies 13D9 and 6B9 are both specific for N-propionylated polysialic acid (NPrPSA); however, while 13D9 is protective against meningitis caused by group B meningococci and Escherichia coli capsular type K1 infection, 6B9 is not. The crystal structures of the Fabs from the two antibodies determined at 2.06 and 2.45 A resolutions, respectively, reveal markedly different combining sites, where only the surface of 13D9 is consistent with the recognition of extended helical epitopes known to exist in the capsular polysaccharides of etiological agents of meningitis. Interestingly, complementarity determining region H2 on 13D9 lies in a non-canonical conformation that docking studies show is a critical feature in the generation of negative free energy of binding. Finally, the model of extended NPrPSA decasaccharide bound to 13D9 derived from docking studies is consistent with saturation transfer difference nuclear magnetic resonance experiments. Together, these results provide further evidence that extended epitopes have the ability to break immune tolerance associated with the polysialic acid capsule of these pathogens.
The antigen-binding site of an N-propionylated polysialic acid-specific antibody protective against group B meningococci is consistent with extended epitopes.,Johal AR, Jarrell HC, Letts JA, Khieu NH, Landry RC, Jachymek W, Yang Q, Jennings HJ, Brisson JR, Evans SV Glycobiology. 2013 Aug;23(8):946-54. doi: 10.1093/glycob/cwt031. Epub 2013 May, 22. PMID:23704298[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Johal AR, Jarrell HC, Letts JA, Khieu NH, Landry RC, Jachymek W, Yang Q, Jennings HJ, Brisson JR, Evans SV. The antigen-binding site of an N-propionylated polysialic acid-specific antibody protective against group B meningococci is consistent with extended epitopes. Glycobiology. 2013 Aug;23(8):946-54. doi: 10.1093/glycob/cwt031. Epub 2013 May, 22. PMID:23704298 doi:10.1093/glycob/cwt031
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