2ARJ

CD8alpha-alpha in complex with YTS 105.18 Fab

2ARJ の概要

• エントリーDOI: 10.2210/pdb2arj/pdb
• 関連するPDBエントリー: 1AKJ 1BQH 1CD8 1NEZ 1Q69
• 分子名称: YTS 105.18 antigen binding region Light chain, YTS 105.18 antigen binding region Heavy chain, T-cell surface glycoprotein CD8 alpha chain, ... (4 entities in total)
• 機能のキーワード: protein-protein complex, antibody fab, immune system, immunoglobulin domain
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P01731
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 120683.41

構造登録者

Shore, D.A.,Teyton, L.,Dwek, R.A.,Rudd, P.M.,Wilson, I.A. (登録日: 2005-08-19, 公開日: 2006-05-30, 最終更新日: 2024-10-30)

主引用文献

Shore, D.A.,Teyton, L.,Dwek, R.A.,Rudd, P.M.,Wilson, I.A.
Crystal structure of the TCR co-receptor CD8alphaalpha in complex with monoclonal antibody YTS 105.18 Fab fragment at 2.88 A resolution.
J.Mol.Biol., 358:347-354, 2006

PubMed Abstract: The CD8 glycoprotein functions as an essential element in the control of T-cell selection, maturation and the TCR-mediated response to peptide antigen. CD8 is expressed as both heterodimeric CD8alphabeta and homodimeric CD8alphaalpha isoforms, which have distinct physiological roles and exhibit tissue-specific expression patterns. CD8alphaalpha has previously been crystallized in complex with class I pMHC and, more recently, with the mouse class Ib thymic leukemia antigen (TL). Here, we present the crystal structure of a soluble form of mouse CD8alphaalpha in complex with rat monoclonal antibody YTS 105.18 Fab fragment at 2.88 A resolution. YTS 105.18, which is commonly used in the blockade of CD8+ T-cell activation in response to peptide antigen, is specific for mouse CD8alpha. The YTS 105.18 Fab is one of only five rat IgG Fab structures to have been reported to date. Analysis of the YTS 105.18 Fab epitope on CD8alpha reveals that this antibody blocks CD8 activity by hydrogen bonding to residues that are critical for interaction with both class I pMHC and TL. Structural comparison of the liganded and unliganded forms of soluble CD8alphaalpha indicates that the mouse CD8alphaalpha immunoglobulin-domain dimer does not undergo significant structural alteration upon interaction either with class I pMHC or TL.

PubMed: 16530222
DOI: 10.1016/j.jmb.2006.02.016

実験手法

X-RAY DIFFRACTION (2.88 Å)