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4KI1

Primitive triclinic crystal form of the human IgE-Fc(epsilon)3-4 bound to its B cell receptor derCD23

Summary for 4KI1
Entry DOI10.2210/pdb4ki1/pdb
Related4EZM
DescriptorIG EPSILON CHAIN C REGION, LOW AFFINITY IMMUNOGLOBULIN EPSILON FC RECEPTOR, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordsimmunoglobulin fold, lectin, antibody receptor, immune system
Biological sourceHomo sapiens (human)
More
Cellular locationCell membrane; Single-pass type II membrane protein: P06734
Total number of polymer chains8
Total formula weight167983.82
Authors
Dhaliwal, B.,Pang, M.O.Y.,Sutton, B.J.,Beavil, A.J. (deposition date: 2013-05-01, release date: 2014-03-05, Last modification date: 2024-11-27)
Primary citationDhaliwal, B.,Pang, M.O.,Yuan, D.,Beavil, A.J.,Sutton, B.J.
A range of C3-C4 interdomain angles in IgE Fc accommodate binding to its receptor CD23.
Acta Crystallogr F Struct Biol Commun, 70:305-309, 2014
Cited by
PubMed Abstract: The antibody IgE plays a central role in allergic disease, functioning principally through two cell-surface receptors: FcℇRI and CD23. FcℇRI on mast cells and basophils mediates the immediate hypersensitivity response, whilst the interaction of IgE with CD23 on B cells regulates IgE production. Crystal structures of the lectin-like `head' domain of CD23 alone and bound to a subfragment of IgE consisting of the dimer of Cℇ3 and Cℇ4 domains (Fcℇ3-4) have recently been determined, revealing flexibility in the IgE-binding site of CD23. Here, a new crystal form of the CD23-Fcℇ3-4 complex with different molecular-packing constraints is reported, which together with the earlier results demonstrates that conformational variability at the interface extends additionally to the IgE Fc and the quaternary structure of its domains.
PubMed: 24598915
DOI: 10.1107/S2053230X14003355
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.2 Å)
Structure validation

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