Structural highlights
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
