4MQ7

Structure of human CD1d-sulfatide

4MQ7 の概要

• エントリーDOI: 10.2210/pdb4mq7/pdb
• 関連するPDBエントリー: 4MNG 4MNH
• 分子名称: Antigen-presenting glycoprotein CD1d, Cd1d1 protein, Beta-2-microglobulin, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: gamma-delta, t cell receptor, humans, t cells, non-classical, lipids, cd1d, restriction, immunoglobulin, major histocompatibility complex, antigen presentation, self-ligands, immune system
• 由来する生物種: Homo sapiens (human, mouse); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 44744.63

構造登録者

Luoma, A.M.,Adams, E.J. (登録日: 2013-09-15, 公開日: 2013-12-18, 最終更新日: 2024-10-30)

主引用文献

Luoma, A.M.,Castro, C.D.,Mayassi, T.,Bembinster, L.A.,Bai, L.,Picard, D.,Anderson, B.,Scharf, L.,Kung, J.E.,Sibener, L.V.,Savage, P.B.,Jabri, B.,Bendelac, A.,Adams, E.J.
Crystal Structure of V delta 1 T Cell Receptor in Complex with CD1d-Sulfatide Shows MHC-like Recognition of a Self-Lipid by Human gamma delta T Cells.
Immunity, 39:1032-1042, 2013

PubMed Abstract: The nature of the antigens recognized by γδ T cells and their potential recognition of major histocompatibility complex (MHC)-like molecules has remained unclear. Members of the CD1 family of lipid-presenting molecules are suggested ligands for Vδ1 TCR-expressing γδ T cells, the major γδ lymphocyte population in epithelial tissues. We crystallized a Vδ1 TCR in complex with CD1d and the self-lipid sulfatide, revealing the unusual recognition of CD1d by germline Vδ1 residues spanning all complementarity-determining region (CDR) loops, as well as sulfatide recognition separately encoded by nongermline CDR3δ residues. Binding and functional analysis showed that CD1d presenting self-lipids, including sulfatide, was widely recognized by gut Vδ1+ γδ T cells. These findings provide structural demonstration of MHC-like recognition of a self-lipid by γδ T cells and reveal the prevalence of lipid recognition by innate-like T cell populations.

PubMed: 24239091
DOI: 10.1016/j.immuni.2013.11.001

実験手法

X-RAY DIFFRACTION (2.6032 Å)