1H9V

Human Fc-gamma-Receptor IIa (FcgRIIa), monoclinic

1H9V の概要

• エントリーDOI: 10.2210/pdb1h9v/pdb
• 関連するPDBエントリー: 1FCG
• 分子名称: LOW AFFINITY IMMUNOGLOBULIN GAMMA FC RECEPTOR II-A (1 entity in total)
• 機能のキーワード: immune system, membrane protein, fcr, fc-receptor, immunoglobulin, fcgr, fc-gamma-r
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cell membrane; Single-pass type I membrane protein: P12318
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19342.65

構造登録者

Sondermann, P.,Kaiser, J.,Jacob, U. (登録日: 2001-03-21, 公開日: 2001-06-21, 最終更新日: 2024-11-20)

主引用文献

Sondermann, P.,Kaiser, J.,Jacob, U.
Molecular Basis for Immune Complex Recognition: A Comparison of Fc-Receptor Structures
J.Mol.Biol., 309:737-, 2001

PubMed Abstract: Once antigen is opsonised by IgG it is removed from the circulation by Fcgamma-receptor expressing cells. Fcgamma-receptors are type I transmembrane molecules that carry extracellular parts consisting of two or three immunoglobulin domains. Previously solved structures of Fc-receptors reveal that the N-terminal two Ig-like domains are arranged in a steep angle forming a heart-shaped structure. The crystal structure of the FcgammaRIII/hIgG1-Fc-fragment demonstrated that the Fc-fragment is recognised through loops of the C-terminal receptor domain of the FcgammaRIII. As the overall structure of the FcRs and their Ig ligands are very similar we modelled the Ig complexes with FcgammaRI, FcgammaRII and FcepsilonRIalpha based on the FcgammaRIII/hIgG1-Fc-fragment structure. The obtained models are consistent with the observed biochemical data and may explain the observed specificity and affinities.

PubMed: 11397093
DOI: 10.1006/JMBI.2001.4670

実験手法

X-RAY DIFFRACTION (3 Å)