Characterization of the human IgE Fc-Fc epsilon RI alpha interaction.
A significant amount of progress has been achieved on characterizing the interaction of the IgE Fc molecule with the Fc epsilon RI alpha. However, there is yet no definitive structural information which precisely defines the nature of this interaction. It is clear that this information will only be provided by the resolution of the X-ray crystallographic structures of the IgE Fc molecule, the Fc epsilon RI alpha subunit extracellular domain, and the IgE Fc-Fc epsilon RI alpha complex. It is anticipated that these structures will be determined in the near future, and that they may provide some insight into the development of potential therapeutics effective in the management of IgE-mediated allergic diseases.
Kochan
J P
JP
Department of Bronchopulmonary Research, Hoffmann-La Roche Inc., Nutley, NJ 07110.
Mallamaci
M
M
Gilfillan
A
A
Madison
V
V
Basu
M
M
D000818:Animals; D001491:Basophils / Q000276:immunology; D001665:Binding Sites; D016466:CHO Cells; D002460:Cell Line; D002522:Chlorocebus aethiops; D006224:Cricetinae; D006801:Humans; D007073:Immunoglobulin E / Q000378:metabolism*; D008407:Mast Cells / Q000276:immunology; D051379:Mice; D008958:Models, Molecular; D010446:Peptide Fragments / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D051381:Rats; D017455:Receptors, IgE / Q000737:chemistry / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism
D010446:Peptide Fragments; D017455:Receptors, IgE; D011993:Recombinant Fusion Proteins; D007073:Immunoglobulin E