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4JKW

Structure of the extracellular domain of butyrophilin BTN3A1 in complex with Isopentenyl pyrophosphate (IPP)

Summary for 4JKW
Entry DOI10.2210/pdb4jkw/pdb
Related4k55
DescriptorButyrophilin subfamily 3 member A1, 3-METHYLBUT-3-ENYL TRIHYDROGEN DIPHOSPHATE (3 entities in total)
Functional Keywordsimmunoglobulin superfamily, immune system
Biological sourceHomo sapiens (human)
Cellular locationCell membrane; Single-pass type I membrane protein: O00481
Total number of polymer chains1
Total formula weight14018.61
Authors
Kumar, A.,Mori, L.,De Libero, G. (deposition date: 2013-03-12, release date: 2013-07-24, Last modification date: 2024-10-09)
Primary citationVavassori, S.,Kumar, A.,Wan, G.S.,Ramanjaneyulu, G.S.,Cavallari, M.,El Daker, S.,Beddoe, T.,Theodossis, A.,Williams, N.K.,Gostick, E.,Price, D.A.,Soudamini, D.U.,Voon, K.K.,Olivo, M.,Rossjohn, J.,Mori, L.,De Libero, G.
Butyrophilin 3A1 binds phosphorylated antigens and stimulates human gamma delta T cells.
Nat.Immunol., 14:908-916, 2013
Cited by
PubMed Abstract: Human T cells that express a T cell antigen receptor (TCR) containing γ-chain variable region 9 and δ-chain variable region 2 (Vγ9Vδ2) recognize phosphorylated prenyl metabolites as antigens in the presence of antigen-presenting cells but independently of major histocompatibility complex (MHC), the MHC class I-related molecule MR1 and antigen-presenting CD1 molecules. Here we used genetic approaches to identify the molecule that binds and presents phosphorylated antigens. We found that the butyrophilin BTN3A1 bound phosphorylated antigens with low affinity, at a stoichiometry of 1:1, and stimulated mouse T cells with transgenic expression of a human Vγ9Vδ2 TCR. The structures of the BTN3A1 distal domain in complex with host- or microbe-derived phosphorylated antigens had an immunoglobulin-like fold in which the antigens bound in a shallow pocket. Soluble Vγ9Vδ2 TCR interacted specifically with BTN3A1-antigen complexes. Accordingly, BTN3A1 represents an antigen-presenting molecule required for the activation of Vγ9Vδ2 T cells.
PubMed: 23872678
DOI: 10.1038/ni.2665
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.01 Å)
Structure validation

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