6Y0M

Crystal structure of human CD23 lectin domain N225D, K229E, S252N, T251N mutant

Summary for 6Y0M

• Entry DOI: 10.2210/pdb6y0m/pdb
• Descriptor: Low affinity immunoglobulin epsilon Fc receptor membrane-bound form (2 entities in total)
• Functional Keywords: antibody receptor, c-type lectin, calcium binding protein, ige, immunoglobulin e, cd23, immune system
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 16205.93

Authors

Ilkow, V.F.,Davies, A.M.,Sutton, B.J.,McDonnell, J.M. (deposition date: 2020-02-09, release date: 2021-06-16, Last modification date: 2024-11-13)

Primary citation

Ilkow, V.F.,Davies, A.M.,Dhaliwal, B.,Beavil, A.J.,Sutton, B.J.,McDonnell, J.M.
Reviving lost binding sites: Exploring calcium-binding site transitions between human and murine CD23.
Febs Open Bio, 11:1827-1840, 2021

PubMed 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 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.

PubMed: 34075727
DOI: 10.1002/2211-5463.13214

Experimental method

X-RAY DIFFRACTION (1.5 Å)