2H2T

CD23 Lectin domain, Calcium 2+-bound

2H2T の概要

• エントリーDOI: 10.2210/pdb2h2t/pdb
• 関連するPDBエントリー: 1HLJ 1KJE 1T8C 1T8D 2H2R
• 分子名称: Low affinity immunoglobulin epsilon Fc receptor (Lymphocyte IgE receptor) (Fc-epsilon-RII) (Immunoglobulin E-binding factor) (CD23 antigen), CALCIUM ION (3 entities in total)
• 機能のキーワード: c-type lectin, calcium-bound, lectin domain, low affinity ige 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: 1
• 化学式量合計: 19555.80

構造登録者

Wurzburg, B.A. (登録日: 2006-05-19, 公開日: 2006-06-20, 最終更新日: 2024-11-13)

主引用文献

Wurzburg, B.A.,Tarchevskaya, S.S.,Jardetzky, T.S.
Structural Changes in the Lectin Domain of CD23, the Low-Affinity IgE Receptor, upon Calcium Binding.
Structure, 14:1049-1058, 2006

PubMed Abstract: CD23, the low-affinity receptor for IgE (Fc epsilonRII), regulates IgE synthesis and also mediates IgE-dependent antigen transport and processing. CD23 is a unique Fc receptor belonging to the C-type lectin-like domain superfamily and binds IgE in an unusual, non-lectin-like manner, requiring calcium but not carbohydrate. We have solved the high-resolution crystal structures of the human CD23 lectin domain in the presence and absence of Ca2+. The crystal structures differ significantly from a previously determined NMR structure and show that calcium binding occurs at the principal binding site, but not at an auxiliary site that appears to be absent in human CD23. Conformational differences between the apo and Ca2+ bound structures suggest how IgE-Fc binding can be both calcium-dependent and carbohydrate-independent.

PubMed: 16765898
DOI: 10.1016/j.str.2006.03.017

実験手法

X-RAY DIFFRACTION (1.3 Å)