2OI9

Structure of the 2C/Ld/QL9 allogeneic complex


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.35 Å
  • R-Value Free: 0.226 
  • R-Value Work: 0.220 
  • R-Value Observed: 0.221 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

How a single T cell receptor recognizes both self and foreign MHC.

Colf, L.A.Bankovich, A.J.Hanick, N.A.Bowerman, N.A.Jones, L.L.Kranz, D.M.Garcia, K.C.

(2007) Cell 129: 135-146

  • DOI: https://doi.org/10.1016/j.cell.2007.01.048
  • Primary Citation of Related Structures:  
    2E7L, 2OI9

  • PubMed Abstract: 

    alphabeta T cell receptors (TCRs) can crossreact with both self- and foreign- major histocompatibility complex (MHC) proteins in an enigmatic phenomenon termed alloreactivity. Here we present the 2.35 A structure of the 2C TCR complexed with its foreign ligand H-2L(d)-QL9. Surprisingly, we find that this TCR utilizes a different strategy to engage the foreign pMHC in comparison to the manner in which it recognizes a self ligand H-2K(b)-dEV8. 2C engages both shared and polymorphic residues on L(d) and K(b), as well as the unrelated QL9 and dEV8 peptide antigens, in unique pair-wise contacts, resulting in greater structural complementarity with the L(d)-QL9 complex. In the structure of an engineered, high-affinity 2C TCR variant bound to H-2L(d)-QL9, the "wild-type" TCR-MHC binding orientation persists despite modified TCR-CDR3alpha interactions with peptide. Thus, a single TCR recognizes two globally similar, but distinct ligands by divergent mechanisms, indicating that receptor-ligand crossreactivity can occur in the absence of molecular mimicry.


  • Organizational Affiliation

    Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Major Histocompatibility Complex protein179Mus musculusMutation(s): 0 
UniProt
Find proteins for P01897 (Mus musculus)
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Go to UniProtKB:  P01897
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UniProt GroupP01897
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
T cell receptor alpha chain113Mus musculusMutation(s): 0 
UniProt
Find proteins for P01738 (Mus musculus)
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Go to UniProtKB:  P01738
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UniProt GroupP01738
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
T cell receptor beta chain121Mus musculusMutation(s): 0 
UniProt
Find proteins for A2NTY6 (Mus musculus)
Explore A2NTY6 
Go to UniProtKB:  A2NTY6
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UniProt GroupA2NTY6
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  • Reference Sequence

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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
peptide (GLN)(LEU)(SER)(PRO)(PHE)(PRO)(PHE)(ASP)(LEU)D [auth Q]9N/AMutation(s): 0 
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.35 Å
  • R-Value Free: 0.226 
  • R-Value Work: 0.220 
  • R-Value Observed: 0.221 
  • Space Group: P 65 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 163.171α = 90
b = 163.171β = 90
c = 95.028γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-04-24
    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