1F2Q

CRYSTAL STRUCTURE OF THE HUMAN HIGH-AFFINITY IGE RECEPTOR

Summary for 1F2Q

• Entry DOI: 10.2210/pdb1f2q/pdb
• Descriptor: HIGH AFFINITY IMMUNOGLOBULIN EPSILON RECEPTOR ALPHA-SUBUNIT, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: immunoglobulin fold, glycoprotein, receptor, ige-binding protein, immune system
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 21857.03

Authors

Garman, S.C.,Kinet, J.P.,Jardetzky, T.S. (deposition date: 2000-05-28, release date: 2000-06-08, Last modification date: 2020-07-29)

Primary citation

Garman, S.C.,Kinet, J.P.,Jardetzky, T.S.
Crystal structure of the human high-affinity IgE receptor.
Cell(Cambridge,Mass.), 95:951-961, 1998

PubMed Abstract: 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.

PubMed: 9875849
DOI: 10.1016/S0092-8674(00)81719-5

Experimental method

X-RAY DIFFRACTION (2.4 Å)