9O61

R-phycoerythrin

9O61 の概要

• エントリーDOI: 10.2210/pdb9o61/pdb
• EMDBエントリー: 70156
• 分子名称: R-phycoerythrin class I alpha subunit, R-phycoerythrin class I beta subunit, PHYCOERYTHROBILIN, ... (4 entities in total)
• 機能のキーワード: t-cell, gamma delta tcr, phycoerythrin, direct, immune system
• 由来する生物種: Pyropia tenera (asakusa nori); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 233941.45

構造登録者

Rashleigh, L.,Venugopal, H.,Rossjohn, J.,Gully, B.S. (登録日: 2025-04-10, 公開日: 2025-08-06, 最終更新日: 2025-10-15)

主引用文献

Rashleigh, L.,Venugopal, H.,Rice, M.T.,Gunasinghe, S.D.,Sok, C.L.,Gherardin, N.A.,Almeida, C.F.,Van Rhijn, I.,Moody, D.B.,Godfrey, D.I.,Rossjohn, J.,Gully, B.S.
Antibody-like recognition of a gamma delta T cell receptor toward a foreign antigen.
Structure, 33:1649-, 2025

PubMed Abstract: The antigen recognition principles of B cells and αβ T cells have been well described compared to those of the γδ T cell. By way of their specificity conferring receptor (γδTCR), γδ T cells can directly bind proteinaceous antigens. A known γδ T cell and B cell model antigen is phycoerythrin (PE), a light harvesting protein from rhodophytes and cyanobacteria. Here we probed human γδTCR reactivity to PE, in which a Vδ1Vγ5 TCR bound directly to induce proximal signaling and cellular activation. We determined the cryoelectron microscopy (cryo-EM) structure of the γδTCR-phycoerythrin immune complex. We then determined the cryo-EM structures of an antibody fragment and an αβTCR bound to PE. This revealed convergent use of apical aromatic residues to mediate contacts with a common PE epitope. Comparative analyses of the γδTCR revealed multiple antibody-like characteristics, including an enrichment of apical aromatic residues. Our findings reveal further distinct facets of antigen recognition by the γδTCR.

PubMed: 40744007
DOI: 10.1016/j.str.2025.07.006

実験手法

ELECTRON MICROSCOPY (1.68 Å)