Crystal structure of the human high-affinity IgE receptor.
Allergic responses result from the activation of mast cells by the human high-affinity IgE receptor. IgE-mediated allergic reactions may develop to a variety of environmental compounds, but the initiation of a response requires the binding of IgE to its high-affinity receptor. We have solved the X-ray crystal structure of the antibody-binding domains of the human IgE receptor at 2.4 A resolution. The structure reveals a highly bent arrangement of immunoglobulin domains that form an extended convex surface of interaction with IgE. A prominent loop that confers specificity for IgE molecules extends from the receptor surface near an unusual arrangement of four exposed tryptophans. The crystal structure of the IgE receptor provides a foundation for the development of new therapeutic approaches to allergy treatment.
Garman
S C
SC
Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA.
Kinet
J P
JP
Jardetzky
T S
TS
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002460:Cell Line; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D006031:Glycosylation; D006801:Humans; D007073:Immunoglobulin E / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D017455:Receptors, IgE / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry; D016415:Sequence Alignment; D012995:Solubility; D014364:Tryptophan
D017455:Receptors, IgE; D011994:Recombinant Proteins; D007073:Immunoglobulin E; D014364:Tryptophan