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PDBsum entry 4y19
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Immune system
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PDB id
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4y19
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Contents |
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179 a.a.
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184 a.a.
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13 a.a.
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205 a.a.
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241 a.a.
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References listed in PDB file
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Key reference
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Title
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T cell receptor reversed polarity recognition of a self-Antigen major histocompatibility complex.
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Authors
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D.X.Beringer,
F.S.Kleijwegt,
F.Wiede,
A.R.Van der slik,
K.L.Loh,
J.Petersen,
N.L.Dudek,
G.Duinkerken,
S.Laban,
A.Joosten,
J.P.Vivian,
Z.Chen,
A.P.Uldrich,
D.I.Godfrey,
J.Mccluskey,
D.A.Price,
K.J.Radford,
A.W.Purcell,
T.Nikolic,
H.H.Reid,
T.Tiganis,
B.O.Roep,
J.Rossjohn.
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Ref.
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Nat Immunol, 2015,
16,
1153-1161.
[DOI no: ]
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PubMed id
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Abstract
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Central to adaptive immunity is the interaction between the αβ T cell receptor
(TCR) and peptide presented by the major histocompatibility complex (MHC)
molecule. Presumably reflecting TCR-MHC bias and T cell signaling constraints,
the TCR universally adopts a canonical polarity atop the MHC. We report the
structures of two TCRs, derived from human induced T regulatory (iTreg) cells,
complexed to an MHC class II molecule presenting a proinsulin-derived peptide.
The ternary complexes revealed a 180° polarity reversal compared to all other
TCR-peptide-MHC complex structures. Namely, the iTreg TCR α-chain and β-chain
are overlaid with the α-chain and β-chain of MHC class II, respectively.
Nevertheless, this TCR interaction elicited a peptide-reactive, MHC-restricted T
cell signal. Thus TCRs are not 'hardwired' to interact with MHC molecules in a
stereotypic manner to elicit a T cell signal, a finding that fundamentally
challenges our understanding of TCR recognition.
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