3AXL

Murine Valpha 10 Vbeta 8.1 T-cell receptor

Summary for 3AXL

• Entry DOI: 10.2210/pdb3axl/pdb
• Descriptor: Valpha 10, Vbeta 8.1 (3 entities in total)
• Functional Keywords: immunoglobulin fold, t-cell receptor, cd1d binding, immune system
• Biological source: Mus musculus (mouse); More
• Total number of polymer chains: 4
• Total formula weight: 97001.11

Authors

Patel, O.,Rossjohn, J. (deposition date: 2011-04-11, release date: 2011-08-03, Last modification date: 2024-10-09)

Primary citation

Uldrich, A.P.,Patel, O.,Cameron, G.,Pellicci, D.G.,Day, E.B.,Sullivan, L.C.,Kyparissoudis, K.,Kjer-Nielsen, L.,Vivian, J.P.,Cao, B.,Brooks, A.G.,Williams, S.J.,Illarionov, P.,Besra, G.S.,Turner, S.J.,Porcelli, S.A.,McCluskey, J.,Smyth, M.J.,Rossjohn, J.,Godfrey, D.I.
A semi-invariant V(alpha)10(+) T cell antigen receptor defines a population of natural killer T cells with distinct glycolipid antigen-recognition properties
Nat.Immunol., 12:616-623, 2011

PubMed Abstract: Type I natural killer T cells (NKT cells) are characterized by an invariant variable region 14-joining region 18 (V(α)14-J(α)18) T cell antigen receptor (TCR) α-chain and recognition of the glycolipid α-galactosylceramide (α-GalCer) restricted to the antigen-presenting molecule CD1d. Here we describe a population of α-GalCer-reactive NKT cells that expressed a canonical V(α)10-J(α)50 TCR α-chain, which showed a preference for α-glucosylceramide (α-GlcCer) and bacterial α-glucuronic acid-containing glycolipid antigens. Structurally, despite very limited TCRα sequence identity, the V(α)10 TCR-CD1d-α-GlcCer complex had a docking mode similar to that of type I TCR-CD1d-α-GalCer complexes, although differences at the antigen-binding interface accounted for the altered antigen specificity. Our findings provide new insight into the structural basis and evolution of glycolipid antigen recognition and have notable implications for the scope and immunological role of glycolipid-specific T cell responses.

PubMed: 21666690
DOI: 10.1038/ni.2051

Experimental method

X-RAY DIFFRACTION (2.9 Å)