4mnh | pdb_00004mnh
Structure of the DP10.7 TCR
Structural highlights
FunctionPublication Abstract from PubMedThe nature of the antigens recognized by gammadelta 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 Vdelta1 TCR-expressing gammadelta T cells, the major gammadelta lymphocyte population in epithelial tissues. We crystallized a Vdelta1 TCR in complex with CD1d and the self-lipid sulfatide, revealing the unusual recognition of CD1d by germline Vdelta1 residues spanning all complementarity-determining region (CDR) loops, as well as sulfatide recognition separately encoded by nongermline CDR3delta residues. Binding and functional analysis showed that CD1d presenting self-lipids, including sulfatide, was widely recognized by gut Vdelta1+ gammadelta T cells. These findings provide structural demonstration of MHC-like recognition of a self-lipid by gammadelta T cells and reveal the prevalence of lipid recognition by innate-like T cell populations. Crystal Structure of Vdelta1 T Cell Receptor in Complex with CD1d-Sulfatide Shows MHC-like Recognition of a Self-Lipid by Human gammadelta T Cells.,Luoma AM, Castro CD, Mayassi T, Bembinster LA, Bai L, Picard D, Anderson B, Scharf L, Kung JE, Sibener LV, Savage PB, Jabri B, Bendelac A, Adams EJ Immunity. 2013 Dec 12;39(6):1032-42. doi: 10.1016/j.immuni.2013.11.001. Epub 2013, Nov 14. PMID:24239091[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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