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PDBsum entry 4p2q
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Immune system
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PDB id
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4p2q
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Contents |
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180 a.a.
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171 a.a.
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14 a.a.
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196 a.a.
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245 a.a.
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13 a.a.
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PDB id:
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Immune system
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Title:
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Crystal structure of the 5cc7 tcr in complex with 5c2/i-ek
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Structure:
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H-2 class ii histocompatibility antigen, e-k alpha chain. Chain: a, f, k, p. Engineered: yes. Mhc class ii e-beta-k. Chain: b, g, l, q. Engineered: yes. 5c2 peptide. Chain: c, h, m, r. Engineered: yes.
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Gene: h2-eb1. Synthetic construct. Organism_taxid: 32630. Expressed in: escherichia coli.
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Resolution:
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3.30Å
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R-factor:
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0.191
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R-free:
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0.236
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Authors:
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M.E.Birnbaum,E.Ozkan,K.C.Garcia
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Key ref:
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M.E.Birnbaum
et al.
(2014).
Deconstructing the peptide-MHC specificity of T cell recognition.
Cell,
157,
1073-1087.
PubMed id:
DOI:
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Date:
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04-Mar-14
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Release date:
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21-May-14
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PROCHECK
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Headers
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References
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P04224
(HA22_MOUSE) -
H-2 class II histocompatibility antigen, E-K alpha chain from Mus musculus
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Seq:
Struc:
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255 a.a.
180 a.a.
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Q31163
(Q31163_MOUSE) -
MHC class II antigen IEk-beta from Mus musculus
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Seq:
Struc:
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263 a.a.
171 a.a.
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No UniProt id for this chain
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No UniProt id for this chain
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DOI no:
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Cell
157:1073-1087
(2014)
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PubMed id:
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Deconstructing the peptide-MHC specificity of T cell recognition.
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M.E.Birnbaum,
J.L.Mendoza,
D.K.Sethi,
S.Dong,
J.Glanville,
J.Dobbins,
E.Ozkan,
M.M.Davis,
K.W.Wucherpfennig,
K.C.Garcia.
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ABSTRACT
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In order to survey a universe of major histocompatibility complex
(MHC)-presented peptide antigens whose numbers greatly exceed the diversity of
the T cell repertoire, T cell receptors (TCRs) are thought to be
cross-reactive. However, the nature and extent of TCR cross-reactivity has not
been conclusively measured experimentally. We developed a system to identify
MHC-presented peptide ligands by combining TCR selection of highly diverse
yeast-displayed peptide-MHC libraries with deep sequencing. Although we
identified hundreds of peptides reactive with each of five different mouse and
human TCRs, the selected peptides possessed TCR recognition motifs that bore a
close resemblance to their known antigens. This structural conservation of the
TCR interaction surface allowed us to exploit deep-sequencing information to
computationally identify activating microbial and self-ligands for human
autoimmune TCRs. The mechanistic basis of TCR cross-reactivity described here
enables effective surveillance of diverse self and foreign antigens without
necessitating degenerate recognition of nonhomologous peptides.
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