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PDBsum entry 4mq7

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Top Page protein ligands Protein-protein interface(s) links
Immune system PDB id
4mq7
Contents
Protein chains
268 a.a.
98 a.a.
Ligands
NAG
CIS
Waters ×85

References listed in PDB file
Key reference
Title Crystal structure of Vδ1 t cell receptor in complex with cd1d-Sulfatide shows mhc-Like recognition of a self-Lipid by human γδ t cells.
Authors A.M.Luoma, C.D.Castro, T.Mayassi, L.A.Bembinster, L.Bai, D.Picard, B.Anderson, L.Scharf, J.E.Kung, L.V.Sibener, P.B.Savage, B.Jabri, A.Bendelac, E.J.Adams.
Ref. Immunity, 2013, 39, 1032-1042. [DOI no: 10.1016/j.immuni.2013.11.001]
PubMed id 24239091
Abstract
The nature of the antigens recognized by γδ T cells and their potential recognition of major histocompatibility complex (MHC)-like molecules has remained unclear. Members of the CD1 family of lipid-presenting molecules are suggested ligands for Vδ1 TCR-expressing γδ T cells, the major γδ lymphocyte population in epithelial tissues. We crystallized a Vδ1 TCR in complex with CD1d and the self-lipid sulfatide, revealing the unusual recognition of CD1d by germline Vδ1 residues spanning all complementarity-determining region (CDR) loops, as well as sulfatide recognition separately encoded by nongermline CDR3δ residues. Binding and functional analysis showed that CD1d presenting self-lipids, including sulfatide, was widely recognized by gut Vδ1+ γδ T cells. These findings provide structural demonstration of MHC-like recognition of a self-lipid by γδ T cells and reveal the prevalence of lipid recognition by innate-like T cell populations.
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