| First Author | Wurzburg BA | Year | 2000 |
| Journal | Immunity | Volume | 13 |
| Issue | 3 | Pages | 375-85 |
| PubMed ID | 11021535 | Mgi Jnum | J:64747 |
| Mgi Id | MGI:1889937 | Doi | 10.1016/s1074-7613(00)00037-6 |
| Citation | Wurzburg BA, et al. (2000) Structure of the human IgE-Fc C epsilon 3-C epsilon 4 reveals conformational flexibility in the antibody effector domains. Immunity 13(3):375-85 |
| abstractText | 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. |
