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PDBsum entry 5w1v
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Immune system
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PDB id
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5w1v
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Contents |
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272 a.a.
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100 a.a.
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201 a.a.
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243 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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A conserved energetic footprint underpins recognition of human leukocyte antigen-E by two distinct αβ t cell receptors.
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Authors
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L.C.Sullivan,
N.G.Walpole,
C.Farenc,
G.Pietra,
M.J.W.Sum,
C.S.Clements,
E.J.Lee,
T.Beddoe,
M.Falco,
M.C.Mingari,
L.Moretta,
S.Gras,
J.Rossjohn,
A.G.Brooks.
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Ref.
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J Biol Chem, 2017,
292,
21149-21158.
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PubMed id
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Abstract
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αβ T cell receptors (TCRs) interact with peptides bound to the polymorphic
major histocompatibility complex class Ia (MHC-Ia) and class II (MHC-II)
molecules as well as the essentially monomorphic MHC class Ib (MHC-Ib)
molecules. Although there is a large amount of information on how TCRs engage
with MHC-Ia and MHC-II, our understanding of TCR/MHC-Ib interactions is very
limited. Infection with cytomegalovirus (CMV) can elicit a CD8+T cell
response restricted by the human MHC-Ib molecule human leukocyte antigen (HLA)-E
and specific for an epitope from UL40 (VMAPRTLIL), which is characterized by
biased TRBV14 gene usage. Here we describe an HLA-E-restricted CD8+T
cell able to recognize an allotypic variant of the UL40 peptide with a
modification at position 8 (P8) of the peptide (VMAPRTLVL) that uses the TRBV9
gene segment. We report the structures of a TRBV9+TCR in complex with
the HLA-E molecule presenting the two peptides. Our data revealed that the
TRBV9+TCR adopts a different docking mode and molecular footprint
atop HLA-E when compared with the TRBV14+TCR-HLA-E ternary complex.
Additionally, despite their differing V gene segment usage and different docking
mechanisms, mutational analyses showed that the TCRs shared a conserved
energetic footprint on the HLA-E molecule, focused around the peptide-binding
groove. Hence, we provide new insights into how monomorphic MHC molecules
interact with T cells.
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