1F6A

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

1F6A の概要

• エントリーDOI: 10.2210/pdb1f6a/pdb
• 関連するPDBエントリー: 1F2Q
• 分子名称: 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)
• 機能のキーワード: immunoglobulin fold, glycoprotein, receptor, ige-binding protein, ige antibody, ige-fc, immune system
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 77388.90

構造登録者

Garman, S.C.,Wurzburg, B.A.,Tarchevskaya, S.S.,Kinet, J.P.,Jardetzky, T.S. (登録日: 2000-06-20, 公開日: 2000-07-20, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.5 Å)