4J6L

Crystal structure of calcium2+-free wild-type CD23 lectin domain (crystal form C)

4J6L の概要

• エントリーDOI: 10.2210/pdb4j6l/pdb
• 関連するPDBエントリー: 4G96
• 分子名称: Low affinity immunoglobulin epsilon Fc receptor (2 entities in total)
• 機能のキーワード: immunoglobulin fold lectin, antibody receptor, immune system
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane; Single-pass type II membrane protein: P06734
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 129319.89

構造登録者

Dhaliwal, B.,Yuan, D.,Sutton, B.J. (登録日: 2013-02-11, 公開日: 2013-08-28, 最終更新日: 2023-09-20)

主引用文献

Dhaliwal, B.,Pang, M.O.,Yuan, D.,Yahya, N.,Fabiane, S.M.,McDonnell, J.M.,Gould, H.J.,Beavil, A.J.,Sutton, B.J.
Conformational plasticity at the IgE-binding site of the B-cell receptor CD23.
Mol.Immunol., 56:693-697, 2013

PubMed Abstract: IgE antibodies play a central role in allergic disease. They recognize allergens via their Fab regions, whilst their effector functions are controlled through interactions of the Fc region with two principal cell surface receptors, FcɛRI and CD23. Crosslinking of FcɛRI-bound IgE on mast cells and basophils by allergen initiates an immediate inflammatory response, while the interaction of IgE with CD23 on B-cells regulates IgE production. We have determined the structures of the C-type lectin "head" domain of CD23 from seven crystal forms. The thirty-five independent structures reveal extensive conformational plasticity in two loops that are critical for IgE binding.

PubMed: 23933509
DOI: 10.1016/j.molimm.2013.07.005

実験手法

X-RAY DIFFRACTION (3.15 Å)