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PDBsum entry 4ozf
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Immune system
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PDB id
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4ozf
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Contents |
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181 a.a.
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181 a.a.
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193 a.a.
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242 a.a.
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13 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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Jr5.1 protein complex
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Structure:
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Hla class ii histocompatibility antigen, dq alpha 1 chain. Chain: a. Synonym: dc-1 alpha chain,dc-alpha,hla-dca,mhc class ii dqa1. Engineered: yes. Hla class ii histocompatibility antigen, dq beta 1 chain. Chain: b. Synonym: mhc class ii antigen. Engineered: yes. T-cell receptor, jr5.1 alpha chain.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: hla-dqa1. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Expression_system_cell_line: hi5. Gene: hla-dqb1. Expressed in: escherichia coli.
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Resolution:
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2.70Å
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R-factor:
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0.186
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R-free:
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0.238
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Authors:
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J.Petersen,H.H.Reid,J.Rossjohn
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Key ref:
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J.Petersen
et al.
(2014).
T-cell receptor recognition of HLA-DQ2-gliadin complexes associated with celiac disease.
Nat Struct Biol,
21,
480-488.
PubMed id:
DOI:
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Date:
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15-Feb-14
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Release date:
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16-Apr-14
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PROCHECK
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Headers
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References
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P01909
(DQA1_HUMAN) -
HLA class II histocompatibility antigen, DQ alpha 1 chain from Homo sapiens
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Seq:
Struc:
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254 a.a.
181 a.a.
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Q5Y7D3
(Q5Y7D3_HUMAN) -
HLA class II histocompatibility antigen DQ beta chain from Homo sapiens
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Seq:
Struc:
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261 a.a.
181 a.a.
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Q2YD82
(Q2YD82_HUMAN) -
TRA@ protein from Homo sapiens
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Seq:
Struc:
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241 a.a.
193 a.a.*
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DOI no:
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Nat Struct Biol
21:480-488
(2014)
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PubMed id:
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T-cell receptor recognition of HLA-DQ2-gliadin complexes associated with celiac disease.
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J.Petersen,
V.Montserrat,
J.R.Mujico,
K.L.Loh,
D.X.Beringer,
M.van Lummel,
A.Thompson,
M.L.Mearin,
J.Schweizer,
Y.Kooy-Winkelaar,
J.van Bergen,
J.W.Drijfhout,
W.T.Kan,
N.L.La Gruta,
R.P.Anderson,
H.H.Reid,
F.Koning,
J.Rossjohn.
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ABSTRACT
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Celiac disease is a T cell-mediated disease induced by dietary gluten, a
component of which is gliadin. 95% of individuals with celiac disease carry the
HLA (human leukocyte antigen)-DQ2 locus. Here we determined the T-cell receptor
(TCR) usage and fine specificity of patient-derived T-cell clones specific for
two epitopes from wheat gliadin, DQ2.5-glia-α1a and DQ2.5-glia-α2. We
determined the ternary structures of four distinct biased TCRs specific for
those epitopes. All three TCRs specific for DQ2.5-glia-α2 docked centrally
above HLA-DQ2, which together with mutagenesis and affinity measurements
provided a basis for the biased TCR usage. A non-germline encoded arginine
residue within the CDR3β loop acted as the lynchpin within this common docking
footprint. Although the TCRs specific for DQ2.5-glia-α1a and DQ2.5-glia-α2
docked similarly, their interactions with the respective gliadin determinants
differed markedly, thereby providing a basis for epitope specificity.
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