1BEC

BETA CHAIN OF A T CELL ANTIGEN RECEPTOR


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Work: 0.198 
  • R-Value Observed: 0.198 

wwPDB Validation   3D Report Full Report


This is version 2.1 of the entry. See complete history


Literature

Crystal structure of the beta chain of a T cell antigen receptor.

Bentley, G.A.Boulot, G.Karjalainen, K.Mariuzza, R.A.

(1995) Science 267: 1984-1987

  • DOI: https://doi.org/10.1126/science.7701320
  • Primary Citation of Related Structures:  
    1BEC

  • PubMed Abstract: 

    The crystal structure of the extracellular portion of the beta chain of a murine T cell antigen receptor (TCR), determined at a resolution of 1.7 angstroms, shows structural homology to immunoglobulins. The structure of the first and second hypervariable loops suggested that, in general, they adopt more restricted sets of conformations in TCR beta chains than those found in immunoglobulins; the third hypervariable loop had certain structural characteristics in common with those of immunoglobulin heavy chain variable domains. The variable and constant domains were in close contact, presumably restricting the flexibility of the beta chain. This may facilitate signal transduction from the TCR to the associated CD3 molecules in the TCR-CD3 complex.


  • Organizational Affiliation

    Unite d'Immunologie Structurale (CNRS URA 359), Institut Pasteur, Paris, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
14.3.D T CELL ANTIGEN RECEPTOR238Mus musculusMutation(s): 0 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Work: 0.198 
  • R-Value Observed: 0.198 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 100.6α = 90
b = 36.6β = 113.4
c = 71.5γ = 90
Software Package:
Software NamePurpose
XDSdata scaling
X-PLORmodel building
PROLSQrefinement
X-PLORrefinement
XDSdata reduction
X-PLORphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1995-10-25
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 2.0: 2019-07-17
    Changes: Atomic model, Data collection, Refinement description
  • Version 2.1: 2019-08-14
    Changes: Advisory, Data collection, Derived calculations, Refinement description