6y0m
From Proteopedia
Crystal structure of human CD23 lectin domain N225D, K229E, S252N, T251N mutant
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). Publication Abstract from PubMedImmunoglobulin E (IgE) is a central regulatory and triggering molecule of allergic immune responses.IgE's interaction with CD23 modulates both IgE production and functional activities.CD23 is a non-canonical immunoglobulin receptor, unrelated to receptors of other antibody isotypes. Human CD23 is a calcium-dependent (C-type) lectin-like domain that has apparently lost its carbohydrate binding capability. The calcium binding site classically required for carbohydrate binding in C-type lectins is absent in human CD23 but is present in the murine molecule.To determine if the absence of this calcium binding site affects the structure and function of human CD23, CD23 mutant proteins with increasingly 'murine-like' sequences were generated. Restoration of the calcium binding site was confirmed by NMR spectroscopy and structures of mutant human CD23 proteins were determined by X-ray crystallography, although no electron density for calcium was observed.This study offers insights into the evolutionary differences between murine and human CD23, and some of the functional differences between CD23 in different species. Reviving lost binding sites: Exploring calcium binding-site transitions between human and murine CD23.,Ilkow VF, Davies AM, Dhaliwal B, Beavil AJ, Sutton BJ, McDonnell JM FEBS Open Bio. 2021 Jun 2. doi: 10.1002/2211-5463.13214. PMID:34075727[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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