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| | ==The complex of human IgE-Fc with two bound Fab fragments== | | ==The complex of human IgE-Fc with two bound Fab fragments== |
| - | <StructureSection load='4j4p' size='340' side='right' caption='[[4j4p]], [[Resolution|resolution]] 2.91Å' scene=''> | + | <StructureSection load='4j4p' size='340' side='right'caption='[[4j4p]], [[Resolution|resolution]] 2.91Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4j4p]] 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=4J4P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J4P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4j4p]] 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=4J4P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J4P 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=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]] 2.91Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lso|1lso]], [[2wqr|2wqr]], [[2y7q|2y7q]]</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='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])</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=4j4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j4p OCA], [https://pdbe.org/4j4p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j4p RCSB], [https://www.ebi.ac.uk/pdbsum/4j4p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j4p 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=4j4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j4p OCA], [http://pdbe.org/4j4p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j4p RCSB], [http://www.ebi.ac.uk/pdbsum/4j4p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j4p ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [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: Drinkwater, N]] | + | [[Category: Large Structures]] |
| - | [[Category: Sutton, B J]] | + | [[Category: Drinkwater N]] |
| - | [[Category: Ig like domain]] | + | [[Category: Sutton BJ]] |
| - | [[Category: Immune system]]
| + | |
| Structural highlights
Function
IGHE_HUMAN
Publication Abstract from PubMed
Crystallographic and solution studies have shown that IgE molecules are acutely bent in their Fc region. Crystal structures reveal the Cvarepsilon2 domain pair folded back onto the Cvarepsilon3-Cvarepsilon4 domains, but is the molecule exclusively bent or can the Cvarepsilon2 domains adopt extended conformations and even 'flip' from one side of the molecule to the other? We report the crystal structure of IgE-Fc captured in a fully extended, symmetrical conformation and show by molecular dynamics, calorimetry, stopped-flow kinetic, surface plasmon resonance (SPR) and Forster resonance energy transfer (FRET) analyses that the antibody can indeed adopt such extended conformations in solution. This diversity of conformational states available to IgE-Fc offers a new perspective on IgE function in allergen recognition, as part of the B-cell receptor and as a therapeutic target in allergic disease.
Human immunoglobulin E flexes between acutely bent and extended conformations.,Drinkwater N, Cossins BP, Keeble AH, Wright M, Cain K, Hailu H, Oxbrow A, Delgado J, Shuttleworth LK, Kao MW, McDonnell JM, Beavil AJ, Henry AJ, Sutton BJ Nat Struct Mol Biol. 2014 Apr;21(4):397-404. doi: 10.1038/nsmb.2795. Epub 2014, Mar 16. PMID:24632569[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Drinkwater N, Cossins BP, Keeble AH, Wright M, Cain K, Hailu H, Oxbrow A, Delgado J, Shuttleworth LK, Kao MW, McDonnell JM, Beavil AJ, Henry AJ, Sutton BJ. Human immunoglobulin E flexes between acutely bent and extended conformations. Nat Struct Mol Biol. 2014 Apr;21(4):397-404. doi: 10.1038/nsmb.2795. Epub 2014, Mar 16. PMID:24632569 doi:http://dx.doi.org/10.1038/nsmb.2795
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