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| | <StructureSection load='5lgk' size='340' side='right'caption='[[5lgk]], [[Resolution|resolution]] 3.50Å' scene=''> | | <StructureSection load='5lgk' size='340' side='right'caption='[[5lgk]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5lgk]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LGK OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LGK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5lgk]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LGK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LGK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 3.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IGHE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), FCER2, CD23A, CLEC4J, FCE2, IGEBF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=5lgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lgk OCA], [http://pdbe.org/5lgk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lgk RCSB], [http://www.ebi.ac.uk/pdbsum/5lgk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lgk 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=5lgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lgk OCA], [https://pdbe.org/5lgk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lgk RCSB], [https://www.ebi.ac.uk/pdbsum/5lgk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lgk ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FCER2_HUMAN FCER2_HUMAN]] Low-affinity receptor for immunoglobulin E (IgE) and CR2/CD21. Has essential roles in the regulation of IgE production and in the differentiation of B-cells (it is a B-cell-specific antigen). | + | [https://www.uniprot.org/uniprot/IGHE_HUMAN IGHE_HUMAN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dhaliwal, B]] | + | [[Category: Dhaliwal B]] |
| - | [[Category: Pang, M O.Y]] | + | [[Category: Pang MOY]] |
| - | [[Category: Sutton, B J]] | + | [[Category: Sutton BJ]] |
| - | [[Category: Antibody receptor]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Immunoglobulin fold lectin]]
| + | |
| Structural highlights
Function
IGHE_HUMAN
Publication Abstract from PubMed
The antibody IgE plays a central role in allergic disease mechanisms. Its effector functions are controlled through interactions between the Fc region and two principal cell surface receptors FcepsilonRI and CD23. The interaction with FcepsilonRI is primarily responsible for allergic sensitization and the inflammatory response, while IgE binding to CD23 is involved in the regulation of IgE synthesis and allergen transcytosis. Here we present the crystal structure of a CD23/IgE-Fc complex and conduct isothermal titration calorimetric binding studies. Two lectin-like "head" domains of CD23 bind to IgE-Fc with affinities that differ by more than an order of magnitude, but the crystal structure reveals only one head bound to one of the two identical heavy-chains in the asymmetrically bent IgE-Fc. These results highlight the subtle interplay between receptor binding sites in IgE-Fc and their affinities, the understanding of which may be exploited for therapeutic intervention in allergic disease.
IgE binds asymmetrically to its B cell receptor CD23.,Dhaliwal B, Pang MO, Keeble AH, James LK, Gould HJ, McDonnell JM, Sutton BJ, Beavil AJ Sci Rep. 2017 Mar 31;7:45533. doi: 10.1038/srep45533. PMID:28361904[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dhaliwal B, Pang MO, Keeble AH, James LK, Gould HJ, McDonnell JM, Sutton BJ, Beavil AJ. IgE binds asymmetrically to its B cell receptor CD23. Sci Rep. 2017 Mar 31;7:45533. doi: 10.1038/srep45533. PMID:28361904 doi:http://dx.doi.org/10.1038/srep45533
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