1FP5
CRYSTAL STRUCTURE ANALYSIS OF THE HUMAN IGE-FC CEPSILON3-CEPSILON4 FRAGMENT.
Summary for 1FP5
| Entry DOI | 10.2210/pdb1fp5/pdb |
| Related | 1F6A |
| Descriptor | IGE HEAVY CHAIN EPSILON-1 (2 entities in total) |
| Functional Keywords | antibody, fc, immunoglobin fold, "closed" ige-fc, immune system |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 24821.02 |
| Authors | Wurzburg, B.A.,Garman, S.C.,Jardetzky, T.S. (deposition date: 2000-08-30, release date: 2000-09-27, Last modification date: 2024-10-30) |
| Primary citation | Wurzburg, B.A.,Garman, S.C.,Jardetzky, T.S. Structure of the human IgE-Fc C epsilon 3-C epsilon 4 reveals conformational flexibility in the antibody effector domains. Immunity, 13:375-385, 2000 Cited by PubMed Abstract: IgE antibodies mediate antiparasitic immune responses and the inflammatory reactions of allergy and asthma. We have solved the crystal structure of the human IgE-Fc Cepsilon3-Cepsilon4 domains to 2.3 A resolution. The structure reveals a large rearrangement of the N-terminal Cepsilon3 domains when compared to related IgG-Fc structures and to the IgE-Fc bound to its high-affinity receptor, FcepsilonRI. The IgE-Fc adopts a more compact, closed configuration that places the two Cepsilon3 domains in close proximity, decreases the size of the interdomain cavity, and obscures part of the FcepsilonRI binding site. IgE-Fc conformational flexibility may be required for interactions with two distinct IgE receptors, and the structure suggests strategies for the design of therapeutic compounds for the treatment of IgE-mediated diseases. PubMed: 11021535DOI: 10.1016/S1074-7613(00)00037-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
Download full validation report
