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2h2t

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Revision as of 08:05, 18 October 2017

CD23 Lectin domain, Calcium 2+-bound

Structural highlights

2h2t is a 1 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:	2h2r, 1t8c, 1t8d, 1kje, 1hlj
Gene:	FCER2 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

CD23, 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.

References

↑ Wurzburg BA, Tarchevskaya SS, Jardetzky TS. Structural changes in the lectin domain of CD23, the low-affinity IgE receptor, upon calcium binding. Structure. 2006 Jun;14(6):1049-58. PMID:16765898 doi:http://dx.doi.org/10.1016/j.str.2006.03.017

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2h2t"

@@ Line 1: / Line 1: @@
 ==CD23 Lectin domain, Calcium 2+-bound==
 <StructureSection load='2h2t' size='340' side='right' caption='[[2h2t]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2h2r|2h2r]], [[1t8c|1t8c]], [[1t8d|1t8d]], [[1kje|1kje]], [[1hlj|1hlj]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FCER2 ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2t OCA], [http://pdbe.org/2h2t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h2t RCSB], [http://www.ebi.ac.uk/pdbsum/2h2t PDBsum]</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=2h2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2t OCA], [http://pdbe.org/2h2t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h2t RCSB], [http://www.ebi.ac.uk/pdbsum/2h2t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2h2t ProSAT]</span></td></tr>
 </table>
 == Function ==

2h2t

From Proteopedia

Revision as of 08:05, 18 October 2017

CD23 Lectin domain, Calcium 2+-bound

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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