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2QRS

Crystal Structure of a single chain trimer composed of the MHC I heavy chain H-2Kb Y84A, beta-2microglobulin, and ovalbumin-derived peptide.

2QRS の概要
エントリーDOI10.2210/pdb2qrs/pdb
関連するPDBエントリー2QRI 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, single chain, ovalbumin, 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93948.55
構造登録者
Mitaksov, V.E.,Fremont, D.H. (登録日: 2007-07-29, 公開日: 2007-11-06, 最終更新日: 2024-11-20)
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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 2qrs
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-06-11に公開中

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