@article{5224bc4ffe754c23ac23b8f2b85624e3,
title = "Reviving lost binding sites: Exploring calcium binding-site transitions between human and murine CD23",
abstract = "Immunoglobulin E (IgE) is a central regulatory and triggering molecule of allergic immune responses. IgE{\textquoteright}s interaction with CD23 modulates both IgE production and functional activities.CD23 is a noncanonical 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 whether 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.",
author = "Veronica Ilkow and Davies, {Anna Marie} and Balvinder Dhaliwal and Andrew Beavil and Brian Sutton and James McDonnell",
note = "Funding Information: We thank the Medical Research Council (UK) for grant support (G1100090). We thank Diamond Light Source for access to beamlines I02 and I04-1 (proposal MX9495) that contributed to the results presented here, and the beamline staff for their assistance. We acknowledge support from the Centre for Biomolecular Spectroscopy, Kings College London, which was established with a Capital Award from the Wellcome Trust (grant number 085944). Funding Information: We thank the Medical Research Council (UK) for grant support (G1100090). We thank Diamond Light Source for access to beamlines I02 and I04‐1 (proposal MX9495) that contributed to the results presented here, and the beamline staff for their assistance. We acknowledge support from the Centre for Biomolecular Spectroscopy, Kings College London, which was established with a Capital Award from the Wellcome Trust (grant number 085944). Publisher Copyright: {\textcopyright} 2021 The Authors. FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies Copyright: Copyright 2021 Elsevier B.V., All rights reserved.",
year = "2021",
month = jul,
doi = "10.1002/2211-5463.13214",
language = "English",
volume = "11",
pages = "1827--1840",
journal = "FEBS Open Bio",
issn = "2211-5463",
publisher = "Wiley-Blackwell",
number = "7",
}