A model of the Fc of human IgE was constructed using the known three-dimensional structure of IgG Fc. On the basis of amino acid sequence homology, the CE2, CE3 and CE4 domains were modelled after CG3, CG2 and CG3, respectively. The mode of association of the CG2 and of the CG3 pairs of domains was assumed for the CE3 and the CE4 pairs, respectively; the CE2 pair of domains was assembled such that they interact like the CG3 domains. An asymmetric linkage is favored for the two inter-epsilon chain disulfide bridges, i.e. the bonds were assumed to be between non-homologous cysteines. The atomic interactions in the interface of the CE2:CE2 and CE4:CE4 domain pairs were computed, and predictions are made on the solvent accessibility of the individual residues in the fragment. The model can be useful in the study of regions that may be involved in the interaction of IgE with Fc(epsilon) receptors.
A model of the Fc of immunoglobulin E.,Padlan EA, Davies DR Mol Immunol. 1986 Oct;23(10):1063-75. PMID:3796618[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Padlan EA, Davies DR. A model of the Fc of immunoglobulin E. Mol Immunol. 1986 Oct;23(10):1063-75. PMID:3796618
