3HUJ

Crystal structure of human CD1d-alpha-Galactosylceramide in complex with semi-invariant NKT cell receptor

Summary for 3HUJ

• Entry DOI: 10.2210/pdb3huj/pdb
• Related: 2po6
• Descriptor: T-cell surface glycoprotein CD1d, Beta-2-microglobulin, NKT15 T cell receptor alpha-chain, ... (10 entities in total)
• Functional Keywords: cd1d, nkt t cell receptor, alpha-galactosylceramide, protein receptor complex, cell membrane, disulfide bond, endosome, glycoprotein, host-virus interaction, immune response, immunoglobulin domain, innate immunity, lysosome, membrane, transmembrane, disease mutation, glycation, mhc i, pyrrolidone carboxylic acid, secreted, immune system
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 8
• Total formula weight: 193820.02

Authors

Pang, S.S. (deposition date: 2009-06-14, release date: 2009-07-28, Last modification date: 2024-11-13)

Primary citation

Pellicci, D.G.,Patel, O.,Kjer-Nielsen, L.,Pang, S.S.,Sullivan, L.C.,Kyparissoudis, K.,Brooks, A.G.,Reid, H.H.,Gras, S.,Lucet, I.S.,Koh, R.,Smyth, M.J.,Mallevaey, T.,Matsuda, J.L.,Gapin, L.,McCluskey, J.,Godfrey, D.I.,Rossjohn, J.
Differential recognition of CD1d-alpha-galactosyl ceramide by the V beta 8.2 and V beta 7 semi-invariant NKT T cell receptors
Immunity, 31:47-59, 2009

PubMed Abstract: The semi-invariant natural killer T cell receptor (NKT TCR) recognizes CD1d-lipid antigens. Although the TCR alpha chain is typically invariant, the beta chain expression is more diverse, where three V beta chains are commonly expressed in mice. We report the structures of V alpha 14-V beta 8.2 and V alpha 14-V beta 7 NKT TCRs in complex with CD1d-alpha-galactosylceramide (alpha-GalCer) and the 2.5 A structure of the human NKT TCR-CD1d-alpha-GalCer complex. Both V beta 8.2 and V beta 7 NKT TCRs and the human NKT TCR ligated CD1d-alpha-GalCer in a similar manner, highlighting the evolutionarily conserved interaction. However, differences within the V beta domains of the V beta 8.2 and V beta 7 NKT TCR-CD1d complexes resulted in altered TCR beta-CD1d-mediated contacts and modulated recognition mediated by the invariant alpha chain. Mutagenesis studies revealed the differing contributions of V beta 8.2 and V beta 7 residues within the CDR2 beta loop in mediating contacts with CD1d. Collectively we provide a structural basis for the differential NKT TCR V beta usage in NKT cells.

PubMed: 19592275
DOI: 10.1016/j.immuni.2009.04.018

Experimental method

X-RAY DIFFRACTION (2.5 Å)