1S7X

Crystal structures of the murine class I major histocompatibility complex H-2Db in complex with LCMV-derived gp33 index peptide and three of its escape variants

1S7X の概要

• エントリーDOI: 10.2210/pdb1s7x/pdb
• 関連するPDBエントリー: 1n5a 1s7q 1s7r 1s7s 1s7t 1s7u 1s7v 1s7w
• 分子名称: H-2 class I histocompatibility antigen, D-B alpha chain, Beta-2-microglobulin, Glycoprotein 9-residue peptide, ... (4 entities in total)
• 機能のキーワード: lcmv, mhc class i, immune escape, immune system
• 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: P01899; Secreted: P01887; Glycoprotein G1: Virion membrane ; Peripheral membrane protein . Glycoprotein G2: Virion membrane ; Single-pass membrane protein . Stable signal peptide: Virion membrane ; Multi-pass membrane protein : P07399
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 204730.88

構造登録者

Velloso, L.M.,Michaelsson, J.,Ljunggren, H.G.,Schneider, G.,Achour, A. (登録日: 2004-01-30, 公開日: 2004-05-04, 最終更新日: 2024-11-06)

主引用文献

Velloso, L.M.,Michaelsson, J.,Ljunggren, H.G.,Schneider, G.,Achour, A.
Determination of structural principles underlying three different modes of lymphocytic choriomeningitis virus escape from CTL recognition.
J.Immunol., 172:5504-5511, 2004

PubMed Abstract: Lymphocytic choriomeningitis virus infection of H-2(b) mice generates a strong CD8(+) CTL response mainly directed toward three immunodominant epitopes, one of which, gp33, is presented by both H-2D(b) and H-2K(b) MHC class I molecules. This CTL response acts as a selective agent for the emergence of viral escape variants. These variants generate altered peptide ligands (APLs) that, when presented by class I MHC molecules, antagonize CTL recognition and ultimately allow the virus to evade the cellular immune response. The emergence of APLs of the gp33 epitope is particularly advantageous for LCMV, as it allows viral escape in the context of both H-2D(b) and H-2K(b) MHC class I molecules. We have determined crystal structures of three different APLs of gp33 in complex with both H-2D(b) and H-2K(b). Comparison between these APL/MHC structures and those of the index gp33 peptide/MHC reveals the structural basis for three different strategies used by LCMV viral escape mutations: 1) conformational changes in peptide and MHC residues that are potential TCR contacts, 2) impairment of APL binding to the MHC peptide binding cleft, and 3) introduction of subtle changes at the TCR/pMHC interface, such as the removal of a single hydroxyl group.

PubMed: 15100292

実験手法

X-RAY DIFFRACTION (2.41 Å)