2QRI

Crystal structure of a single chain trimer composed of the MHC I heavy chain H-2Kb WT, beta-2microglobulin, and ovalbumin-derived peptide.

2QRI の概要

• エントリーDOI: 10.2210/pdb2qri/pdb
• 関連するPDBエントリー: 2QRS 2QRT
• 分子名称: H-2 class I histocompatibility antigen K-B alpha chain, Beta-2 microglobulin, ovalbumin-derived peptide (2 entities in total)
• 機能のキーワード: mhc-i, ova, single chain mhc-i, glycoprotein, immune response, membrane, mhc i, transmembrane, immune system
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 94132.74

構造登録者

Mitaksov, V.E.,Fremont, D.H. (登録日: 2007-07-28, 公開日: 2007-11-06, 最終更新日: 2023-08-30)

主引用文献

Mitaksov, V.,Truscott, S.M.,Lybarger, L.,Connolly, J.M.,Hansen, T.H.,Fremont, D.H.
Structural engineering of pMHC reagents for T cell vaccines and diagnostics.
Chem.Biol., 14:909-922, 2007

PubMed Abstract: MHC class I peptide complexes (pMHC) are routinely used to enumerate T cell populations and are currently being evaluated as vaccines to tumors and specific pathogens. Herein, we describe the structures of three generations of single-chain pMHC progressively designed for the optimal presentation of covalently associated epitopes. Our ultimate design employs a versatile disulfide trap between an invariant MHC residue and a short C-terminal peptide extension. This general strategy is nondisruptive of native pMHC conformation and T cell receptor engagement. Indeed, cell-surface-expressed MHC complexes with disulfide-trapped epitopes are refractory to peptide exchange, suggesting they will make safe and effective vaccines. Furthermore, we find that disulfide-trap stabilized, recombinant pMHC reagents reliably detect polyclonal CD8 T cell populations as proficiently as conventional reagents and are thus well suited to monitor or modulate immune responses during pathogenesis.

PubMed: 17719490
DOI: 10.1016/j.chembiol.2007.07.010

実験手法

X-RAY DIFFRACTION (2 Å)