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4WW1

Crystal structure of human TCR Alpha Chain-TRAV21-TRAJ8 and Beta Chain-TRBV7-8

Summary for 4WW1
Entry DOI10.2210/pdb4ww1/pdb
Related4WW2
DescriptorTCR Alpha Chain-TRAV21-TRAJ8, TCR Beta Chain-TRBV7-8 (3 entities in total)
Functional Keywordsimmunity, nkt cells, immune system
Biological sourceHomo sapiens
More
Total number of polymer chains2
Total formula weight49942.34
Authors
Le Nours, J.,Praveena, T.,Pellicci, D.G.,Lim, R.T.,Besra, G.,Howell, A.R.,Godfrey, D.I.,Rossjohn, J.,Uldrich, A.P. (deposition date: 2014-11-10, release date: 2016-02-03, Last modification date: 2024-10-23)
Primary citationLe Nours, J.,Praveena, T.,Pellicci, D.G.,Gherardin, N.A.,Ross, F.J.,Lim, R.T.,Besra, G.S.,Keshipeddy, S.,Richardson, S.K.,Howell, A.R.,Gras, S.,Godfrey, D.I.,Rossjohn, J.,Uldrich, A.P.
Atypical natural killer T-cell receptor recognition of CD1d-lipid antigens.
Nat Commun, 7:10570-10570, 2016
Cited by
PubMed Abstract: Crucial to Natural Killer T (NKT) cell function is the interaction between their T-cell receptor (TCR) and CD1d-antigen complex. However, the diversity of the NKT cell repertoire and the ensuing interactions with CD1d-antigen remain unclear. We describe an atypical population of CD1d-α-galactosylceramide (α-GalCer)-reactive human NKT cells that differ markedly from the prototypical TRAV10-TRAJ18-TRBV25-1(+) type I NKT cell repertoire. These cells express a range of TCR α- and β-chains that show differential recognition of glycolipid antigens. Two atypical NKT TCRs (TRAV21-TRAJ8-TRBV7-8 and TRAV12-3-TRAJ27-TRBV6-5) bind orthogonally over the A'-pocket of CD1d, adopting distinct docking modes that contrast with the docking mode of all type I NKT TCR-CD1d-antigen complexes. Moreover, the interactions with α-GalCer differ between the type I and these atypical NKT TCRs. Accordingly, diverse NKT TCR repertoire usage manifests in varied docking strategies and specificities towards CD1d-α-GalCer and related antigens, thus providing far greater scope for diverse glycolipid antigen recognition.
PubMed: 26875526
DOI: 10.1038/ncomms10570
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.38 Å)
Structure validation

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