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PDBsum entry 2eys
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Immune system
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PDB id
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2eys
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References listed in PDB file
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Key reference
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Title
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A structural basis for selection and cross-Species reactivity of the semi-Invariant nkt cell receptor in cd1d/glycolipid recognition.
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Authors
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L.Kjer-Nielsen,
N.A.Borg,
D.G.Pellicci,
T.Beddoe,
L.Kostenko,
C.S.Clements,
N.A.Williamson,
M.J.Smyth,
G.S.Besra,
H.H.Reid,
M.Bharadwaj,
D.I.Godfrey,
J.Rossjohn,
J.Mccluskey.
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Ref.
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J Exp Med, 2006,
203,
661-673.
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PubMed id
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Abstract
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Little is known regarding the basis for selection of the semi-invariant
alphabeta T cell receptor (TCR) expressed by natural killer T (NKT) cells or how
this mediates recognition of CD1d-glycolipid complexes. We have determined the
structures of two human NKT TCRs that differ in their CDR3beta composition and
length. Both TCRs contain a conserved, positively charged pocket at the ligand
interface that is lined by residues from the invariant TCR alpha- and
semi-invariant beta-chains. The cavity is centrally located and ideally suited
to interact with the exposed glycosyl head group of glycolipid antigens.
Sequences common to mouse and human invariant NKT TCRs reveal a contiguous
conserved "hot spot" that provides a basis for the reactivity of NKT cells
across species. Structural and functional data suggest that the CDR3beta loop
provides a plasticity mechanism that accommodates recognition of a variety of
glycolipid antigens presented by CD1d. We propose a model of NKT
TCR-CD1d-glycolipid interaction in which the invariant CDR3alpha loop is
predicted to play a major role in determining the inherent bias toward CD1d. The
findings define a structural basis for the selection of the semi-invariant
alphabeta TCR and the unique antigen specificity of NKT cells.
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