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4ki1

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==Primitive triclinic crystal form of the human IgE-Fc(epsilon)3-4 bound to its B cell receptor derCD23==
==Primitive triclinic crystal form of the human IgE-Fc(epsilon)3-4 bound to its B cell receptor derCD23==
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<StructureSection load='4ki1' size='340' side='right' caption='[[4ki1]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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<StructureSection load='4ki1' size='340' side='right'caption='[[4ki1]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4ki1]] is a 8 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=4KI1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KI1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4ki1]] is a 8 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=4KI1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KI1 FirstGlance]. <br>
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</td></tr><tr><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><br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ezm|4ezm]]</td></tr>
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<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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr><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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ki1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ki1 OCA], [https://pdbe.org/4ki1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ki1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ki1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ki1 ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ki1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ki1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ki1 RCSB], [http://www.ebi.ac.uk/pdbsum/4ki1 PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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[https://www.uniprot.org/uniprot/IGHE_HUMAN IGHE_HUMAN]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The antibody IgE plays a central role in allergic disease, functioning principally through two cell-surface receptors: FcRI and CD23. FcRI on mast cells and basophils mediates the immediate hypersensitivity response, whilst the interaction of IgE with CD23 on B cells regulates IgE production. Crystal structures of the lectin-like `head' domain of CD23 alone and bound to a subfragment of IgE consisting of the dimer of C3 and C4 domains (Fc3-4) have recently been determined, revealing flexibility in the IgE-binding site of CD23. Here, a new crystal form of the CD23-Fc3-4 complex with different molecular-packing constraints is reported, which together with the earlier results demonstrates that conformational variability at the interface extends additionally to the IgE Fc and the quaternary structure of its domains.
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A range of C3-C4 interdomain angles in IgE Fc accommodate binding to its receptor CD23.,Dhaliwal B, Pang MO, Yuan D, Beavil AJ, Sutton BJ Acta Crystallogr F Struct Biol Commun. 2014 Mar;70(Pt 3):305-9. doi:, 10.1107/S2053230X14003355. Epub 2014 Feb 20. PMID:24598915<ref>PMID:24598915</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4ki1" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[CD23|CD23]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Beavil, A J.]]
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[[Category: Large Structures]]
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[[Category: Dhaliwal, B.]]
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[[Category: Beavil AJ]]
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[[Category: Pang, M O.Y.]]
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[[Category: Dhaliwal B]]
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[[Category: Sutton, B J.]]
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[[Category: Pang MOY]]
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[[Category: Antibody receptor]]
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[[Category: Sutton BJ]]
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[[Category: Immune system]]
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[[Category: Immunoglobulin fold]]
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[[Category: Lectin]]
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Current revision

Primitive triclinic crystal form of the human IgE-Fc(epsilon)3-4 bound to its B cell receptor derCD23

PDB ID 4ki1

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