2h2t: Difference between revisions
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<StructureSection load='2h2t' size='340' side='right'caption='[[2h2t]], [[Resolution|resolution]] 1.30Å' scene=''> | <StructureSection load='2h2t' size='340' side='right'caption='[[2h2t]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2h2t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2h2t]] is a 1 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=2H2T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H2T FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=2h2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2t OCA], [https://pdbe.org/2h2t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h2t RCSB], [https://www.ebi.ac.uk/pdbsum/2h2t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h2t 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=2h2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2t OCA], [https://pdbe.org/2h2t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h2t RCSB], [https://www.ebi.ac.uk/pdbsum/2h2t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h2t ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://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). | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Wurzburg | [[Category: Wurzburg BA]] | ||
Latest revision as of 12:51, 30 August 2023
CD23 Lectin domain, Calcium 2+-boundCD23 Lectin domain, Calcium 2+-bound
Structural highlights
FunctionFCER2_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). 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 PubMedCD23, the low-affinity receptor for IgE (Fc epsilonRII), regulates IgE synthesis and also mediates IgE-dependent antigen transport and processing. CD23 is a unique Fc receptor belonging to the C-type lectin-like domain superfamily and binds IgE in an unusual, non-lectin-like manner, requiring calcium but not carbohydrate. We have solved the high-resolution crystal structures of the human CD23 lectin domain in the presence and absence of Ca2+. The crystal structures differ significantly from a previously determined NMR structure and show that calcium binding occurs at the principal binding site, but not at an auxiliary site that appears to be absent in human CD23. Conformational differences between the apo and Ca2+ bound structures suggest how IgE-Fc binding can be both calcium-dependent and carbohydrate-independent. Structural changes in the lectin domain of CD23, the low-affinity IgE receptor, upon calcium binding.,Wurzburg BA, Tarchevskaya SS, Jardetzky TS Structure. 2006 Jun;14(6):1049-58. PMID:16765898[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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