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Instruments / Technical Area	Publication Details	Published
I02-Macromolecular Crystallography I04-1-Macromolecular Crystallography (fixed wavelength)	Reviving lost binding sites: Exploring calcium binding‐site transitions between human and murine CD23 Veronica F. Ilkow , Anna M. Davies , Balvinder Dhaliwal , Andrew J. Beavil , Brian J. Sutton , James M. Mcdonnell Febs Open Bio DOI: 10.1002/2211-5463.13214 Diamond Proposal Number(s): [9495] Open Access Show Abstract ▼ Abstract: Immunoglobulin 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.	Jun 2021
I04-1-Macromolecular Crystallography (fixed wavelength)	Crystal structures of the human IgD Fab reveal insights into CH1 domain diversity Anna M. Davies , Rebecca L. Beavil , Momchil Barbolov , Balraj S. Sandhar , Hannah J. Gould , Andrew J. Beavil , Brian Sutton , James M. Mcdonnell Molecular Immunology 159, 28 - 37 DOI: 10.1016/j.molimm.2023.05.006 Diamond Proposal Number(s): [25301] Open Access Show Abstract ▼ Abstract: Antibodies of the IgD isotype remain the least well characterized of the mammalian immunoglobulin isotypes. Here we report three-dimensional structures for the Fab region of IgD, based on four different crystal structures, at resolutions of 1.45–2.75 Å. These IgD Fab crystals provide the first high-resolution views of the unique Cδ1 domain. Structural comparisons identify regions of conformational diversity within the Cδ1 domain, as well as among the homologous domains of Cα1, Cγ1 and Cμ1. The IgD Fab structure also possesses a unique conformation of the upper hinge region, which may contribute to the overall disposition of the very long linker sequence between the Fab and Fc regions found in human IgD. Structural similarities observed between IgD and IgG, and differences with IgA and IgM, are consistent with predicted evolutionary relationships for the mammalian antibody isotypes.	Jul 2023
I24-Microfocus Macromolecular Crystallography	Expanding the anti-Phl p 7 antibody toolkit: an anti-idiotype nanobody inhibitor Susan K. Vester , Anna M. Davies , Rebecca L. Beavil , Balraj S. Sandhar , Andrew J. Beavil , Hannah J. Gould , Brian Sutton , James M. Mcdonnell Antibodies 12 DOI: 10.3390/antib12040075 Diamond Proposal Number(s): [25301] Open Access Show Abstract ▼ Abstract: We have previously produced a toolkit of antibodies, comprising recombinant human antibodies of all but one of the human isotypes, directed against the polcalcin family antigen Phl p 7. In this work, we complete the toolkit of human antibody isotypes with the IgD version of the anti-Phl p 7 monoclonal antibody. We also raised a set of nanobodies against the IgD anti-Phl p 7 antibody and identify and characterize one paratope-specific nanobody. This nanobody also binds to the IgE isotype of this antibody, which shares the same idiotype, and orthosterically inhibits the interaction with Phl p 7. The 2.1 Å resolution X-ray crystal structure of the nanobody in complex with the IgD Fab is described.	Nov 2023

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