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PDBsum entry 4n0c
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Immune system
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PDB id
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4n0c
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Contents |
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173 a.a.
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195 a.a.
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239 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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Structural interplay between germline interactions and adaptive recognition determines the bandwidth of tcr-Peptide-Mhc cross-Reactivity.
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Authors
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J.J.Adams,
S.Narayanan,
M.E.Birnbaum,
S.S.Sidhu,
S.J.Blevins,
M.H.Gee,
L.V.Sibener,
B.M.Baker,
D.M.Kranz,
K.C.Garcia.
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Ref.
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Nat Immunol, 2016,
17,
87-94.
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PubMed id
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Abstract
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The T cell antigen receptor (TCR)-peptide-major histocompatibility complex (MHC)
interface is composed of conserved and diverse regions, yet the relative
contribution of each in shaping recognition by T cells remains unclear. Here we
isolated cross-reactive peptides with limited homology, which allowed us to
compare the structural properties of nine peptides for a single TCR-MHC pair.
The TCR's cross-reactivity was rooted in highly similar recognition of an apical
'hot-spot' position in the peptide with tolerance of sequence variation at
ancillary positions. Furthermore, we found a striking structural convergence
onto a germline-mediated interaction between the TCR CDR1α region and the MHC
α2 helix in twelve TCR-peptide-MHC complexes. Our studies suggest that TCR-MHC
germline-mediated constraints, together with a focus on a small peptide hot
spot, might place limits on peptide antigen cross-reactivity.
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