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| | <StructureSection load='2y7q' size='340' side='right'caption='[[2y7q]], [[Resolution|resolution]] 3.40Å' scene=''> | | <StructureSection load='2y7q' size='340' side='right'caption='[[2y7q]], [[Resolution|resolution]] 3.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2y7q]] is a 3 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=2Y7Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y7Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2y7q]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y7Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y7Q FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </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>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fp5|1fp5]], [[1f6a|1f6a]], [[1j87|1j87]], [[1o0v|1o0v]], [[1j88|1j88]], [[1j86|1j86]], [[1j89|1j89]], [[1g84|1g84]], [[1ige|1ige]], [[1rpq|1rpq]], [[1f2q|1f2q]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fp5|1fp5]], [[1f6a|1f6a]], [[1j87|1j87]], [[1o0v|1o0v]], [[1j88|1j88]], [[1j86|1j86]], [[1j89|1j89]], [[1g84|1g84]], [[1ige|1ige]], [[1rpq|1rpq]], [[1f2q|1f2q]]</div></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=2y7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y7q OCA], [http://pdbe.org/2y7q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2y7q RCSB], [http://www.ebi.ac.uk/pdbsum/2y7q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2y7q 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=2y7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y7q OCA], [https://pdbe.org/2y7q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y7q RCSB], [https://www.ebi.ac.uk/pdbsum/2y7q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y7q ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FCERA_HUMAN FCERA_HUMAN]] Binds to the Fc region of immunoglobulins epsilon. High affinity receptor. Responsible for initiating the allergic response. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators (such as histamine) responsible for the manifestations of allergy. The same receptor also induces the secretion of important lymphokines. | + | [[https://www.uniprot.org/uniprot/FCERA_HUMAN FCERA_HUMAN]] Binds to the Fc region of immunoglobulins epsilon. High affinity receptor. Responsible for initiating the allergic response. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators (such as histamine) responsible for the manifestations of allergy. The same receptor also induces the secretion of important lymphokines. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Structural highlights
2y7q is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , |
| Related: | 1fp5, 1f6a, 1j87, 1o0v, 1j88, 1j86, 1j89, 1g84, 1ige, 1rpq, 1f2q |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[FCERA_HUMAN] Binds to the Fc region of immunoglobulins epsilon. High affinity receptor. Responsible for initiating the allergic response. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators (such as histamine) responsible for the manifestations of allergy. The same receptor also induces the secretion of important lymphokines.
Publication Abstract from PubMed
Among antibody classes, IgE has a uniquely slow dissociation rate from, and high affinity for, its cell surface receptor FcvarepsilonRI. We show the structural basis for these key determinants of the ability of IgE to mediate allergic hypersensitivity through the 3.4-A-resolution crystal structure of human IgE-Fc (consisting of the Cvarepsilon2, Cvarepsilon3 and Cvarepsilon4 domains) bound to the extracellular domains of the FcvarepsilonRI alpha chain. Comparison with the structure of free IgE-Fc (reported here at a resolution of 1.9 A) shows that the antibody, which has a compact, bent structure before receptor engagement, becomes even more acutely bent in the complex. Thermodynamic analysis indicates that the interaction is entropically driven, which explains how the noncontacting Cvarepsilon2 domains, in place of the flexible hinge region of IgG antibodies, contribute together with the conformational changes to the unique binding properties of IgE.
Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcvarepsilonRI.,Holdom MD, Davies AM, Nettleship JE, Bagby SC, Dhaliwal B, Girardi E, Hunt J, Gould HJ, Beavil AJ, McDonnell JM, Owens RJ, Sutton BJ Nat Struct Mol Biol. 2011 May;18(5):571-6. Epub 2011 Apr 24. PMID:21516097[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Holdom MD, Davies AM, Nettleship JE, Bagby SC, Dhaliwal B, Girardi E, Hunt J, Gould HJ, Beavil AJ, McDonnell JM, Owens RJ, Sutton BJ. Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcvarepsilonRI. Nat Struct Mol Biol. 2011 May;18(5):571-6. Epub 2011 Apr 24. PMID:21516097 doi:10.1038/nsmb.2044
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