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PDBsum entry 5ivx
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Immune system
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PDB id
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5ivx
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Contents |
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274 a.a.
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99 a.a.
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194 a.a.
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234 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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Crystal structure of b4.2.3 t-cell receptor and h2-dd p18-i10 complex
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Structure:
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H-2 class i histocompatibility antigen, d-d alpha chain. Chain: a. Synonym: h-2d(d). Engineered: yes. Beta-2-microglobulin. Chain: b. Engineered: yes. T-cell receptor alpha chain. Chain: e.
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Gene: h2-d1. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: b2m. Strain: balb/c. Cell_line: b4.2.3 t cell hybridoma.
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Resolution:
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2.10Å
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R-factor:
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0.182
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R-free:
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0.220
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Authors:
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K.Natarajan,J.Jiang,D.Margulies
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Key ref:
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K.Natarajan
et al.
(2017).
An allosteric site in the T-cell receptor Cβ domain plays a critical signalling role.
Nat Commun,
8,
15260.
PubMed id:
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Date:
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21-Mar-16
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Release date:
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29-Mar-17
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PROCHECK
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Headers
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References
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P01900
(HA12_MOUSE) -
H-2 class I histocompatibility antigen, D-D alpha chain from Mus musculus
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Seq:
Struc:
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365 a.a.
274 a.a.*
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P01887
(B2MG_MOUSE) -
Beta-2-microglobulin from Mus musculus
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Seq:
Struc:
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119 a.a.
99 a.a.
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Nat Commun
8:15260
(2017)
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PubMed id:
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An allosteric site in the T-cell receptor Cβ domain plays a critical signalling role.
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K.Natarajan,
A.C.McShan,
J.Jiang,
V.K.Kumirov,
R.Wang,
H.Zhao,
P.Schuck,
M.E.Tilahun,
L.F.Boyd,
J.Ying,
A.Bax,
D.H.Margulies,
N.G.Sgourakis.
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ABSTRACT
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The molecular mechanism through which the interaction of a clonotypic αβ
T-cell receptor (TCR) with a peptide-loaded major histocompatibility complex
(p/MHC) leads to T-cell activation is not yet fully understood. Here we exploit
a high-affinity TCR (B4.2.3) to examine the structural changes that accompany
binding to its p/MHC ligand (P18-I10/H2-Dd). In addition to
conformational changes in complementarity-determining regions (CDRs) of the TCR
seen in comparison of unliganded and bound X-ray structures, NMR
characterization of the TCR β-chain dynamics reveals significant chemical shift
effects in sites removed from the MHC-binding site. Remodelling of electrostatic
interactions near the Cβ H3 helix at the membrane-proximal face of the TCR, a
region implicated in interactions with the CD3 co-receptor, suggests a possible
role for an allosteric mechanism in TCR signalling. The contribution of these
TCR residues to signal transduction is supported by mutagenesis and T-cell
functional assays.
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