2Y7Q

THE HIGH-AFFINITY COMPLEX BETWEEN IGE AND ITS RECEPTOR FC EPSILON RI

Summary for 2Y7Q

• Entry DOI: 10.2210/pdb2y7q/pdb
• Related: 1F2Q 1F6A 1FP5 1G84 1IGE 1J86 1J87 1J88 1J89 1O0V 1RPQ
• Descriptor: HIGH AFFINITY IMMUNOGLOBULIN EPSILON RECEPTOR SUBUNIT ALPHA, IG EPSILON CHAIN C REGION, alpha-D-mannopyranose-(1-3)-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 Keywords: allergy, antibody, ige-binding protein, high-affinity receptor, immunoglobulin c region, immune system
• Biological source: HOMO SAPIENS (HUMAN); More
• Total number of polymer chains: 3
• Total formula weight: 95843.97

Authors

Davies, A.M.,Holdom, M.D.,Nettleship, J.E.,Beavil, A.J.,Owens, R.J.,Sutton, B.J. (deposition date: 2011-02-01, release date: 2011-04-20, Last modification date: 2024-10-23)

Primary citation

Holdom, M.D.,Davies, A.M.,Nettleship, J.E.,Bagby, S.C.,Dhaliwal, B.,Girardi, E.,Hunt, J.,Gould, H.J.,Beavil, A.J.,Mcdonnell, J.M.,Owens, R.J.,Sutton, B.J.
Conformational Changes in Ige Contribute to its Uniquely Slow Dissociation Rate from Receptor Fceri
Nat.Struct.Mol.Biol., 18:571-, 2011

PubMed Abstract: Among antibody classes, IgE has a uniquely slow dissociation rate from, and high affinity for, its cell surface receptor FcɛRI. We show the structural basis for these key determinants of the ability of IgE to mediate allergic hypersensitivity through the 3.4-Å-resolution crystal structure of human IgE-Fc (consisting of the Cɛ2, Cɛ3 and Cɛ4 domains) bound to the extracellular domains of the FcɛRI α chain. Comparison with the structure of free IgE-Fc (reported here at a resolution of 1.9 Å) shows that the antibody, which has a compact, bent structure before receptor engagement, becomes even more acutely bent in the complex. Thermodynamic analysis indicates that the interaction is entropically driven, which explains how the noncontacting Cɛ2 domains, in place of the flexible hinge region of IgG antibodies, contribute together with the conformational changes to the unique binding properties of IgE.

PubMed: 21516097
DOI: 10.1038/NSMB.2044

Experimental method

X-RAY DIFFRACTION (3.4 Å)