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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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PDB id:
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| Name: |
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Immune system
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Title:
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Structure of the hla-e-vmaprtlil/gf4 tcr complex
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Structure:
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Hla class i histocompatibility antigen, alpha chain e. Chain: a, f, k, p. Synonym: mhc class i antigen e. Engineered: yes. Beta-2-microglobulin. Chain: b, g, l, q. Engineered: yes. Vmaprtlil peptide from cmv gpul40. Chain: c, h, m, r.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: hla-e, hla-6.2, hlae. Expressed in: escherichia coli. Expression_system_taxid: 866768. Gene: b2m, cdabp0092, hdcma22p. Human herpesvirus 5 strain ad169. Organism_taxid: 10360.
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Resolution:
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3.31Å
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R-factor:
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0.228
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R-free:
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0.268
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Authors:
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S.Gras,N.Walpole,C.Farenc,J.Rossjohn
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Key ref:
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L.C.Sullivan
et al.
(2017).
A conserved energetic footprint underpins recognition of human leukocyte antigen-E by two distinct αβ T cell receptors.
J Biol Chem,
292,
21149-21158.
PubMed id:
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Date:
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04-Jun-17
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Release date:
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04-Oct-17
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PROCHECK
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Headers
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References
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P13747
(HLAE_HUMAN) -
HLA class I histocompatibility antigen, alpha chain E from Homo sapiens
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Seq:
Struc:
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358 a.a.
272 a.a.*
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P61769
(B2MG_HUMAN) -
Beta-2-microglobulin from Homo sapiens
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Seq:
Struc:
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119 a.a.
100 a.a.*
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J Biol Chem
292:21149-21158
(2017)
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PubMed id:
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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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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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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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