1FP5

CRYSTAL STRUCTURE ANALYSIS OF THE HUMAN IGE-FC CEPSILON3-CEPSILON4 FRAGMENT.

1FP5 の概要

• エントリーDOI: 10.2210/pdb1fp5/pdb
• 関連するPDBエントリー: 1F6A
• 分子名称: IGE HEAVY CHAIN EPSILON-1 (2 entities in total)
• 機能のキーワード: antibody, fc, immunoglobin fold, "closed" ige-fc, immune system
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24821.02

構造登録者

Wurzburg, B.A.,Garman, S.C.,Jardetzky, T.S. (登録日: 2000-08-30, 公開日: 2000-09-27, 最終更新日: 2024-10-30)

主引用文献

Wurzburg, B.A.,Garman, S.C.,Jardetzky, T.S.
Structure of the human IgE-Fc C epsilon 3-C epsilon 4 reveals conformational flexibility in the antibody effector domains.
Immunity, 13:375-385, 2000

PubMed Abstract: IgE antibodies mediate antiparasitic immune responses and the inflammatory reactions of allergy and asthma. We have solved the crystal structure of the human IgE-Fc Cepsilon3-Cepsilon4 domains to 2.3 A resolution. The structure reveals a large rearrangement of the N-terminal Cepsilon3 domains when compared to related IgG-Fc structures and to the IgE-Fc bound to its high-affinity receptor, FcepsilonRI. The IgE-Fc adopts a more compact, closed configuration that places the two Cepsilon3 domains in close proximity, decreases the size of the interdomain cavity, and obscures part of the FcepsilonRI binding site. IgE-Fc conformational flexibility may be required for interactions with two distinct IgE receptors, and the structure suggests strategies for the design of therapeutic compounds for the treatment of IgE-mediated diseases.

PubMed: 11021535
DOI: 10.1016/S1074-7613(00)00037-6

実験手法

X-RAY DIFFRACTION (2.3 Å)