4J6Q
Crystal structure of calcium2+-free wild-type CD23 lectin domain (crystal form G)
Summary for 4J6Q
| Entry DOI | 10.2210/pdb4j6q/pdb |
| Related | 4G96 |
| Descriptor | Low affinity immunoglobulin epsilon Fc receptor (2 entities in total) |
| Functional Keywords | immunoglobulin fold lectin, antibody receptor, immune system |
| Biological source | Homo sapiens (human) |
| Cellular location | Cell membrane; Single-pass type II membrane protein: P06734 |
| Total number of polymer chains | 1 |
| Total formula weight | 16164.99 |
| Authors | Dhaliwal, B.,Pang, M.O.Y.,Sutton, B.J. (deposition date: 2013-02-11, release date: 2013-08-28, Last modification date: 2024-11-20) |
| Primary citation | Dhaliwal, B.,Pang, M.O.,Yuan, D.,Yahya, N.,Fabiane, S.M.,McDonnell, J.M.,Gould, H.J.,Beavil, A.J.,Sutton, B.J. Conformational plasticity at the IgE-binding site of the B-cell receptor CD23. Mol.Immunol., 56:693-697, 2013 Cited by PubMed 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. PubMed: 23933509DOI: 10.1016/j.molimm.2013.07.005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.539 Å) |
Structure validation
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