4KI1
Primitive triclinic crystal form of the human IgE-Fc(epsilon)3-4 bound to its B cell receptor derCD23
Summary for 4KI1
Entry DOI | 10.2210/pdb4ki1/pdb |
Related | 4EZM |
Descriptor | IG 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 Keywords | immunoglobulin fold, lectin, antibody receptor, immune system |
Biological source | Homo sapiens (human) More |
Cellular location | Cell membrane; Single-pass type II membrane protein: P06734 |
Total number of polymer chains | 8 |
Total formula weight | 167983.82 |
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 citation | Dhaliwal, 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: 24598915DOI: 10.1107/S2053230X14003355 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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