2NX5

Crystal structure of ELS4 TCR bound to HLA-B*3501 presenting EBV peptide EPLPQGQLTAY at 1.7A


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.327 
  • R-Value Work: 0.269 
  • R-Value Observed: 0.272 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule

Tynan, F.E.Reid, H.H.Kjer-Nielsen, L.Miles, J.J.Wilce, M.C.Kostenko, L.Borg, N.A.Williamson, N.A.Beddoe, T.Purcell, A.W.Burrows, S.R.McCluskey, J.Rossjohn, J.

(2007) Nat Immunol 8: 268-276

  • DOI: https://doi.org/10.1038/ni1432
  • Primary Citation of Related Structures:  
    2NW2, 2NW3, 2NX5

  • PubMed Abstract: 

    Plasticity of the T cell receptor (TCR) is a hallmark of major histocompatibility complex (MHC)-restricted T cell recognition. However, it is unclear whether interactions of TCR and peptide-MHC class I (pMHCI) always conform to this paradigm. Here we describe the structure of a TCR, ELS4, in its non-ligand-bound form and in complex with a prominent 'bulged' Epstein-Barr virus peptide bound to HLA-B(*)3501. This complex was atypical of previously characterized TCR-pMHCI interactions in that a rigid face of the TCR crumpled the bulged antigenic determinant. This peptide 'bulldozing' created a more featureless pMHCI determinant, allowing the TCR to maximize MHC class I contacts essential for MHC class I restriction of TCR recognition. Our findings represent a mechanism of antigen recognition whereby the plasticity of the T cell response is dictated mainly by adjustments in the MHC-bound peptide.


  • Organizational Affiliation

    Protein Crystallography Unit, Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton, Victoria 3800, Australia.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
HLA-B35A,
F,
K,
P [auth Q]
276Homo sapiensMutation(s): 0 
Gene Names: B-3501
UniProt & NIH Common Fund Data Resources
Find proteins for P01889 (Homo sapiens)
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PHAROS:  P01889
GTEx:  ENSG00000234745 
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UniProt GroupP01889
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-2-microglobulinB,
G,
L,
Q [auth R]
99Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P61769 (Homo sapiens)
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PHAROS:  P61769
GTEx:  ENSG00000166710 
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UniProt GroupP61769
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  • Reference Sequence

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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
EBV peptide, EPLPQGQLTAYC,
H,
M,
R [auth S]
11N/AMutation(s): 0 
UniProt
Find proteins for P03206 (Epstein-Barr virus (strain B95-8))
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UniProt GroupP03206
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
ELS4 TCR alpha chainD,
I,
N,
S [auth T]
188Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P01848 (Homo sapiens)
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PHAROS:  P01848
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  • Reference Sequence
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
ELS4 TCR beta chainE,
J,
O [auth P],
T [auth U]
243Homo sapiensMutation(s): 0 
UniProt
Find proteins for P01850 (Homo sapiens)
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Go to UniProtKB:  P01850
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UniProt GroupP01850
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.327 
  • R-Value Work: 0.269 
  • R-Value Observed: 0.272 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 118.479α = 90
b = 118.067β = 96.04
c = 131.465γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
PDB_EXTRACTdata extraction

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-02-27
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-10-25
    Changes: Data collection, Database references, Refinement description