Figure 6 - A germline-encoded surface is required for recognition of CD1d-glycolipid complexes.


From the following article

Germline-encoded recognition of diverse glycolipids by natural killer T cells

James P Scott-Browne, Jennifer L Matsuda, Thierry Mallevaey, Janice White, Natalie A Borg, James McCluskey, Jamie Rossjohn, John Kappler, Philippa Marrack & Laurent Gapin

Nature Immunology 8, 1105 - 1113 (2007) Published online: 9 September 2007

doi:10.1038/ni1510

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(a) Predicted surface CDR map of Valpha14i-DObeta TCR (far left; CDR loop colors, key). Because the CDR3beta loop of the human Valpha24i-NKT15 TCR that has been crystallized is longer than that of DO-11.10, the TCRbeta chain from the Valpha24i-Vbeta11 TCR iNKT (Protein Data Bank accession code, 2CDE), which has the same CDR3beta length as that of DObeta, was modeled onto the Valpha24i-NKT15 TCR from the TCR–CD1d–alpha-GalCer crystal structure. Individual DO-11.10 CDR3beta residues were then replaced in the Valpha24i-2CDE model for the surface map. In the TCR surfaces identified by mutational analysis (right), residues required for the recognition of glycolipids alpha-GalCer, GSL-1' and iGb3 retain their CDR loop colors from the structure at left; residues with no affect on recognition when substituted with alanine are dark gray; and residues not substituted are light gray. (b) Surface map of the human Valpha24i-NKT15 TCR (left) predicted from the TCR–CD1d–alpha-GalCer crystal structure. In the TCR surface identified by crystallographic analysis (right), residues that make direct contact with CD1d–alpha-GalCer retain their CDR loop color as in the structure at left; residues that do not make contact with CD1d–alpha-GalCer are dark gray; and residues not in the CDR loops are light gray.

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