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Article

BTN3A1 Discriminates γδ T Cell Phosphoantigens from Nonantigenic Small Molecules via a Conformational Sensor in Its B30.2 Domain.

ACS chemical biology - 20 Oct 2017

Salim Mahboob, Knowles Timothy J, Baker Alfie T, Davey Martin S, Jeeves Mark, Sridhar Pooja, Wilkie John, Willcox Carrie R, Kadri Hachemi, Taher Taher E, Vantourout Pierre, Hayday Adrian, Mehellou Youcef, Mohammed Fiyaz, Willcox Benjamin E

Abstract excerpt

Human Vγ9/Vδ2 T-cells detect tumor cells and microbial infections by recognizing small phosphorylated prenyl metabolites termed phosphoantigens (P-Ag). The type-1 transmembrane protein Butyrophilin 3A1 (BTN3A1) is critical to the P-Ag-mediated activation of Vγ9/Vδ2 T-cells; however, the molecular mechanisms involved in BTN3A1-mediated metabolite sensing are unclear, including how P-Ag's are discriminated from...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 28862425
DOI: 10.1021/acschembio.7b00694
PMCID: PMC6558274

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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BTN3A1 Discriminates γδ T Cell Phosphoantigens from Nonantigenic Small Molecules via a Conformational Sensor in Its B30.2 Domain.PMID 28862425Read ↗

The intracellular B30.2 domain of butyrophilin 3A1 binds phosphoantigens to mediate activation of human Vγ9Vδ2 T cells.Semantic proximity Read ↗

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