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PDBsum entry 4y1a
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Immune system
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PDB id
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4y1a
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Contents |
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178 a.a.
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184 a.a.
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14 a.a.
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205 a.a.
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240 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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Immune complex
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Structure:
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Hla class ii histocompatibility antigen, dr alpha chain. Chain: a. Fragment: unp residues 26-206. Synonym: mhc class ii antigen dra. Engineered: yes. Hla class ii histocompatibility antigen, drb1-4 beta chain. Chain: b. Fragment: unp residues 30-219. Synonym: mhc class ii antigen drb1 4,Dr4.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: hla-dra, hla-dra1. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293s. Gene: hla-drb1. Synthetic: yes.
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Resolution:
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4.00Å
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R-factor:
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0.227
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R-free:
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0.283
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Authors:
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D.X.Beringer,J.P.Vivian,H.H.Reid,J.Rossjohn
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Key ref:
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D.X.Beringer
et al.
(2015).
T cell receptor reversed polarity recognition of a self-antigen major histocompatibility complex.
Nat Immunol,
16,
1153-1161.
PubMed id:
DOI:
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Date:
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07-Feb-15
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Release date:
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23-Sep-15
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PROCHECK
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Headers
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References
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P01903
(DRA_HUMAN) -
HLA class II histocompatibility antigen, DR alpha chain from Homo sapiens
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Seq:
Struc:
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254 a.a.
178 a.a.
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P01911
(2B1F_HUMAN) -
HLA class II histocompatibility antigen, DRB1 beta chain from Homo sapiens
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Seq:
Struc:
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266 a.a.
184 a.a.*
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P01308
(INS_HUMAN) -
Insulin from Homo sapiens
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Seq:
Struc:
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110 a.a.
14 a.a.
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DOI no:
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Nat Immunol
16:1153-1161
(2015)
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PubMed id:
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T cell receptor reversed polarity recognition of a self-antigen major histocompatibility complex.
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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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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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