6QZA

HLA-DR1 with GMF Influenza PB1 Peptide

これはPDB形式変換不可エントリーです。

6QZA の概要

• エントリーDOI: 10.2210/pdb6qza/pdb
• 関連するPDBエントリー: 6FUN 6QZC 6QZD 6R0E
• 分子名称: HLA class II histocompatibility antigen, DR alpha chain, HLA class II histocompatibility antigen, DRB1-1 beta chain, PB1-410-422-GMF-Peptide (3 entities in total)
• 機能のキーワード: hla-dr1, cd4, t-cell, influenza, polymerase basic-1, conserved, epitopes, immune system
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 91257.31

構造登録者

Greenshields-Watson, A.,Rizkallah, P.J. (登録日: 2019-03-11, 公開日: 2020-07-15, 最終更新日: 2024-10-16)

主引用文献

Greenshields-Watson, A.,Attaf, M.,MacLachlan, B.J.,Whalley, T.,Rius, C.,Wall, A.,Lloyd, A.,Hughes, H.,Strange, K.E.,Mason, G.H.,Schauenburg, A.J.,Hulin-Curtis, S.L.,Geary, J.,Chen, Y.,Lauder, S.N.,Smart, K.,Vijaykrishna, D.,Grau, M.L.,Shugay, M.,Andrews, R.,Dolton, G.,Rizkallah, P.J.,Gallimore, A.M.,Sewell, A.K.,Godkin, A.J.,Cole, D.K.
CD4+T Cells Recognize Conserved Influenza A Epitopes through Shared Patterns of V-Gene Usage and Complementary Biochemical Features.
Cell Rep, 32:107885-107885, 2020

PubMed Abstract: T cell recognition of peptides presented by human leukocyte antigens (HLAs) is mediated by the highly variable T cell receptor (TCR). Despite this built-in TCR variability, individuals can mount immune responses against viral epitopes by using identical or highly related TCRs expressed on CD8 T cells. Characterization of these TCRs has extended our understanding of the molecular mechanisms that govern the recognition of peptide-HLA. However, few examples exist for CD4 T cells. Here, we investigate CD4 T cell responses to the internal proteins of the influenza A virus that correlate with protective immunity. We identify five internal epitopes that are commonly recognized by CD4 T cells in five HLA-DR1 subjects and show conservation across viral strains and zoonotic reservoirs. TCR repertoire analysis demonstrates several shared gene usage biases underpinned by complementary biochemical features evident in a structural comparison. These epitopes are attractive targets for vaccination and other T cell therapies.

PubMed: 32668259
DOI: 10.1016/j.celrep.2020.107885

実験手法

X-RAY DIFFRACTION (3.09 Å)