1KB5

MURINE T-CELL RECEPTOR VARIABLE DOMAIN/FAB COMPLEX


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Work: 0.219 
  • R-Value Observed: 0.221 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

The three-dimensional structure of a T-cell antigen receptor V alpha V beta heterodimer reveals a novel arrangement of the V beta domain.

Housset, D.Mazza, G.Gregoire, C.Piras, C.Malissen, B.Fontecilla-Camps, J.C.

(1997) EMBO J 16: 4205-4216

  • DOI: https://doi.org/10.1093/emboj/16.14.4205
  • Primary Citation of Related Structures:  
    1KB5

  • PubMed Abstract: 

    The crystal structure of a mouse T-cell antigen receptor (TCR) Fv fragment complexed to the Fab fragment of a specific anti-clonotypic antibody has been determined to 2.6 A resolution. The polypeptide backbone of the TCR V alpha domain is very similar to those of other crystallographically determined V alphas, whereas the V beta structure is so far unique among TCR V beta domains in that it displays a switch of the c" strand from the inner to the outer beta-sheet. The beta chain variable region of this TCR antigen-binding site is characterized by a rather elongated third complementarity-determining region (CDR3beta) that packs tightly against the CDR3 loop of the alpha chain, without leaving any intervening hydrophobic pocket. Thus, the conformation of the CDR loops with the highest potential diversity distinguishes the structure of this TCR antigen-binding site from those for which crystallographic data are available. On the basis of all these results, we infer that a significant conformational change of the CDR3beta loop found in our TCR is required for binding to its cognate peptide-MHC ligand.


  • Organizational Affiliation

    Laboratoire de Cristallographie et Cristallogénèse des Protéines, Institut de Biologie Structurale Jean-Pierre Ebel CEA-CNRS, Grenoble, France.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
KB5-C20 T-CELL ANTIGEN RECEPTOR115Mus musculusMutation(s): 0 
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
KB5-C20 T-CELL ANTIGEN RECEPTOR117Mus musculusMutation(s): 0 
UniProt
Find proteins for P04214 (Mus musculus)
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UniProt GroupP04214
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
ANTIBODY DESIRE-1C [auth L]214Mus musculusMutation(s): 0 
UniProt
Find proteins for P01837 (Mus musculus)
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UniProt GroupP01837
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
ANTIBODY DESIRE-1D [auth H]219Mus musculusMutation(s): 0 
UniProt
Find proteins for P01865 (Mus musculus)
Explore P01865 
Go to UniProtKB:  P01865
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UniProt GroupP01865
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Work: 0.219 
  • R-Value Observed: 0.221 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 187.31α = 90
b = 80.95β = 90
c = 52.08γ = 90
Software Package:
Software NamePurpose
XDSdata scaling
XSCALEdata scaling
AMoREphasing
REFMACrefinement
XDSdata reduction

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-04-08
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-04-04
    Changes: Data collection
  • Version 1.4: 2018-04-11
    Changes: Data collection
  • Version 1.5: 2023-08-09
    Changes: Database references, Refinement description