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Conformational plasticity at the IgE-binding site of the B-cell receptor CD23

DOI: 10.1016/j.molimm.2013.07.005 DOI Help
PMID: 23933509 PMID Help

Authors: Balvinder Dhaliwal (King's College London) , Marie O. Y. Pang (King's College London; MRC & Asthma UK Centre in Allergic Mechanisms of Asthma) , Daopeng Yuan (King's College London; MRC & Asthma UK Centre in Allergic Mechanisms of Asthma) , Norhakim Yahya (King's College London; MRC & Asthma UK Centre in Allergic Mechanisms of Asthma) , Stella Fabiane (King's College London) , James M. Mcdonnell (Kings College London, U.K.) , Hannah J. Gould (Kings College London, U.K.) , Andrew J. Beavil (King's College London) , Brian J. Sutton (King's College London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Molecular Immunology , VOL 56 (4) , PAGES 693 - 697

State: Published (Approved)
Published: December 2013

Open Access Open Access

Abstract: IgE antibodies play a central role in allergic disease. They recognize allergens via their Fab regions, whilst their effector functions are controlled through interactions of the Fc region with two principal cell surface receptors, FcɛRI and CD23. Crosslinking of FcɛRI-bound IgE on mast cells and basophils by allergen initiates an immediate inflammatory response, while the interaction of IgE with CD23 on B-cells regulates IgE production. We have determined the structures of the C-type lectin “head” domain of CD23 from seven crystal forms. The thirty-five independent structures reveal extensive conformational plasticity in two loops that are critical for IgE binding.

Journal Keywords: Binding; Crystallography; X-Ray; Humans; Immunoglobulin; Models; Molecular; Protein; Secondary; Protein; Tertiary; Receptors; Antigen; B-Cell; Receptors; IgE

Subject Areas: Biology and Bio-materials, Medicine


Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography , I04-Macromolecular Crystallography , I24-Microfocus Macromolecular Crystallography

Added On: 14/08/2013 09:26

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