An X-ray Vision for Phosphoantigen Recognition

Michael L Dustin; Emmanuel Scotet; Daniel Olive

doi:10.1016/j.immuni.2019.03.015

An X-ray Vision for Phosphoantigen Recognition

Immunity. 2019 Apr 16;50(4):1026-1028. doi: 10.1016/j.immuni.2019.03.015.

Authors

Michael L Dustin¹, Emmanuel Scotet², Daniel Olive³

Affiliations

¹ Kennedy Institute of Rheumatology, University of Oxford, Oxford, UK. Electronic address: [email protected].
² CRCINA, INSERM, CNRS, Université d'Angers, Université de Nantes, Nantes, France.
³ CRCM, Immunity and Cancer Team, Institut Paoli-Calmettes, INSERM, CNRS, Aix Marseille Université, Marseille, France.

PMID: 30995494
DOI: 10.1016/j.immuni.2019.03.015

Abstract

Invariant Vγ9Vδ2 T cells respond to "phosphoantigen" metabolites through binding to the B30.2 domain of butyrophilin BTN3A. Yang et al. (2019) use molecular dynamic simulations based on X-ray structures of distinct B30.2 domain dimers to identify the asymmetric dimer as most active, which has implications for the inside-out signaling mechanism.

Publication types

Comment

MeSH terms

Antigens, CD*
Butyrophilins
Lymphocyte Activation*
T-Lymphocytes / immunology
X-Rays

Substances

Antigens, CD
Butyrophilins