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PDBsum entry 4n0c
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Immune system
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PDB id
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4n0c
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Contents |
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173 a.a.
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195 a.a.
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239 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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42f3 tcr pcpe3/h-2ld complex
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Structure:
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H-2 class i histocompatibility antigen, l-d alpha chain. Chain: a, e. Fragment: unp residues 25-203. Engineered: yes. Mutation: yes. Pcpe3. Chain: b, f. Engineered: yes. 42f3 vmch alpha.
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Gene: h2-l. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: synthetic peptide. Mus musculus, homo sapiens.
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Resolution:
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2.90Å
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R-factor:
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0.195
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R-free:
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0.247
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Authors:
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M.E.Birnbaum,J.J.Adams,K.C.Garcia
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Key ref:
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J.J.Adams
et al.
(2016).
Structural interplay between germline interactions and adaptive recognition determines the bandwidth of TCR-peptide-MHC cross-reactivity.
Nat Immunol,
17,
87-94.
PubMed id:
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Date:
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01-Oct-13
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Release date:
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19-Aug-15
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PROCHECK
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Headers
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References
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P01897
(HA1L_MOUSE) -
H-2 class I histocompatibility antigen, L-D alpha chain from Mus musculus
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Seq:
Struc:
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362 a.a.
173 a.a.*
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A0A0G2JFA3
(A0A0G2JFA3_MOUSE) -
T cell receptor alpha joining 58 (Fragment) from Mus musculus
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Seq:
Struc:
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21 a.a.
195 a.a.*
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P01738
(TVA1_MOUSE) -
T-cell receptor alpha chain V region PHDS58 from Mus musculus
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Seq:
Struc:
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130 a.a.
195 a.a.*
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P01848
(TCA_HUMAN) -
T cell receptor alpha chain constant from Homo sapiens
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Seq:
Struc:
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140 a.a.
195 a.a.*
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Nat Immunol
17:87-94
(2016)
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PubMed id:
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Structural interplay between germline interactions and adaptive recognition determines the bandwidth of TCR-peptide-MHC cross-reactivity.
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J.J.Adams,
S.Narayanan,
M.E.Birnbaum,
S.S.Sidhu,
S.J.Blevins,
M.H.Gee,
L.V.Sibener,
B.M.Baker,
D.M.Kranz,
K.C.Garcia.
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ABSTRACT
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The T cell antigen receptor (TCR)-peptide-major histocompatibility complex (MHC)
interface is composed of conserved and diverse regions, yet the relative
contribution of each in shaping recognition by T cells remains unclear. Here we
isolated cross-reactive peptides with limited homology, which allowed us to
compare the structural properties of nine peptides for a single TCR-MHC pair.
The TCR's cross-reactivity was rooted in highly similar recognition of an apical
'hot-spot' position in the peptide with tolerance of sequence variation at
ancillary positions. Furthermore, we found a striking structural convergence
onto a germline-mediated interaction between the TCR CDR1α region and the MHC
α2 helix in twelve TCR-peptide-MHC complexes. Our studies suggest that TCR-MHC
germline-mediated constraints, together with a focus on a small peptide hot
spot, might place limits on peptide antigen cross-reactivity.
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