Interaction of IgE with its high-affinity receptor. Structural basis and requirements for effective cross-linking.
Structural interactions between IgE and its high-affinity receptor have been investigated with the methods of fluorescence resonance energy transfer and genetic engineering. The results indicate that IgE has a bent conformation when bound to receptor on the cell surface and that the site of interaction is contained in the C epsilon 2 and C epsilon 3 domains; the C-terminal domain, C epsilon 4, is not required for binding. Cross-linking of IgE-receptor complexes is required for signal transduction across the plasma membrane. Binding studies with defined bivalent ligands indicate that structural and/or kinetic features determine the functional effectiveness of the cross-linked states.
Baird
B
B
Department of Chemistry, Baker Laboratory, Cornell University, Ithaca, N.Y.
Shopes
R J
RJ
Oi
V T
VT
Erickson
J
J
Kane
P
P
Holowka
D
D
D000818:Animals; D000944:Antigens, Differentiation, B-Lymphocyte / Q000502:physiology*; D003432:Cross-Linking Reagents; D004252:DNA Mutational Analysis; D007073:Immunoglobulin E / Q000502:physiology*; D008407:Mast Cells / Q000502:physiology*; D011487:Protein Conformation; D051381:Rats; D011961:Receptors, Fc / Q000502:physiology*; D017455:Receptors, IgE; D011994:Recombinant Proteins / Q000378:metabolism; D013329:Structure-Activity Relationship; D014407:Tumor Cells, Cultured
D000944:Antigens, Differentiation, B-Lymphocyte; D003432:Cross-Linking Reagents; D011961:Receptors, Fc; D017455:Receptors, IgE; D011994:Recombinant Proteins; D007073:Immunoglobulin E