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| | <StructureSection load='3ijs' size='340' side='right'caption='[[3ijs]], [[Resolution|resolution]] 2.55Å' scene=''> | | <StructureSection load='3ijs' size='340' side='right'caption='[[3ijs]], [[Resolution|resolution]] 2.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ijs]] is a 4 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=3IJS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3IJS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ijs]] 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=3IJS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IJS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=GP4:GLUCOSAMINE+4-PHOSPHATE'>GP4</scene>, <scene name='pdbligand=KDO:3-DEOXY-D-MANNO-OCT-2-ULOSONIC+ACID'>KDO</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]] 2.55Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ijh|3ijh]], [[3ijy|3ijy]], [[3ikc|3ikc]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GP4:GLUCOSAMINE+4-PHOSPHATE'>GP4</scene>, <scene name='pdbligand=KDO:3-DEOXY-D-MANNO-OCT-2-ULOSONIC+ACID'>KDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3ijs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ijs OCA], [http://pdbe.org/3ijs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ijs RCSB], [http://www.ebi.ac.uk/pdbsum/3ijs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ijs 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=3ijs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ijs OCA], [https://pdbe.org/3ijs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ijs RCSB], [https://www.ebi.ac.uk/pdbsum/3ijs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ijs ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
| - | [[Category: Blackler, R J]] | + | [[Category: Blackler RJ]] |
| - | [[Category: Brooks, C L]] | + | [[Category: Brooks CL]] |
| - | [[Category: Evans, S V]] | + | [[Category: Evans SV]] |
| - | [[Category: Antibody]]
| + | |
| - | [[Category: Carbohydrate]]
| + | |
| - | [[Category: Chlamydia]]
| + | |
| - | [[Category: Fab]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Kdo]]
| + | |
| - | [[Category: Lp]]
| + | |
| 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 PubMed
In order to explore the structural basis for adaptability in near germline monoclonal antibodies (mAb), we have examined the specificity of the promiscuous mAb S67-27 to both naturally derived carbohydrate antigens and a variety of synthetic nonnatural antigens based on the bacterial lipopolysaccharide component 3-deoxy-alpha-D-manno-oct-2-ulosonic acid (Kdo). One such analog, a 7-O-methyl (7-O-Me) Kdo disaccharide, was found to bind to the antibody with at least 30-fold higher affinity than any other antigen tested. The structure of S67-27 in complex with this analog and three other naturally occurring Kdo antigens revealed that the enhanced affinity of the mAb for the synthetic analog was accomplished by the strategic positioning of CDR H3 away from a conserved Kdo binding pocket that allowed the formation of new antibody-antigen contacts. Furthermore, the comparison of this structure with the structures of related mAbs revealed how the position and structure of CDR H3 influence the specificity or promiscuity of near-germline carbohydrate-recognizing antibodies by altering the architecture of the combining site.
The role of CDR H3 in antibody recognition of a synthetic analog of a lipopolysaccharide antigen.,Brooks CL, Blackler RJ, Sixta G, Kosma P, Muller-Loennies S, Brade L, Hirama T, MacKenzie CR, Brade H, Evans SV Glycobiology. 2010 Feb;20(2):138-47. Epub 2009 Sep 18. PMID:19767317[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Brooks CL, Blackler RJ, Sixta G, Kosma P, Muller-Loennies S, Brade L, Hirama T, MacKenzie CR, Brade H, Evans SV. The role of CDR H3 in antibody recognition of a synthetic analog of a lipopolysaccharide antigen. Glycobiology. 2010 Feb;20(2):138-47. Epub 2009 Sep 18. PMID:19767317 doi:10.1093/glycob/cwp150
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