1F6A

Structure of the human ige-fc bound to its high affinity receptor fc(epsilon)ri(alpha)

Summary for 1F6A

• Entry DOI: 10.2210/pdb1f6a/pdb
• Related: 1F2Q
• Descriptor: HIGH AFFINITY IMMUNOGLOBULIN EPSILON RECEPTOR ALPHA-SUBUNIT, IG EPSILON CHAIN C REGION, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• Functional Keywords: immunoglobulin fold, glycoprotein, receptor, ige-binding protein, ige antibody, ige-fc, immune system
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 3
• Total formula weight: 77388.90

Authors

Garman, S.C.,Wurzburg, B.A.,Tarchevskaya, S.S.,Kinet, J.P.,Jardetzky, T.S. (deposition date: 2000-06-20, release date: 2000-07-20, Last modification date: 2024-10-30)

Primary citation

Garman, S.C.,Wurzburg, B.A.,Tarchevskaya, S.S.,Kinet, J.P.,Jardetzky, T.S.
Structure of the Fc fragment of human IgE bound to its high-affinity receptor Fc (epsilon) RI (alpha).
Nature, 406:259-266, 2000

PubMed Abstract: The initiation of immunoglobulin-E (IgE)-mediated allergic responses requires the binding of IgE antibody to its high-affinity receptor, Fc epsilonRI. Crosslinking of Fc epsilonRI initiates an intracellular signal transduction cascade that triggers the release of mediators of the allergic response. The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI is a key recognition event of this process and involves the extracellular domains of the Fc epsilonRI alpha-chain. To understand the structural basis for this interaction, we have solved the crystal structure of the human IgE-Fc-Fc epsilonRI alpha complex to 3.5-A resolution. The crystal structure reveals that one receptor binds one dimeric IgE-Fc molecule asymmetrically through interactions at two sites, each involving one C epsilon3 domain of the IgE-Fc. The interaction of one receptor with the IgE-Fc blocks the binding of a second receptor, and features of this interaction are conserved in other members of the Fc receptor family. The structure suggests new approaches to inhibiting the binding of IgE to Fc epsilonRI for the treatment of allergy and asthma.

PubMed: 10917520
DOI: 10.1038/35018500

Experimental method

X-RAY DIFFRACTION (3.5 Å)