1OAZ

IgE Fv SPE7 complexed with a recombinant thioredoxin

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.78 Å
  • R-Value Free: 0.276 
  • R-Value Work: 0.208 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history. 


Literature

Antibody Multispecificity Mediated by Conformational Diversity

James, L.C., Roversi, P., Tawfik, D.

(2003) Science 299: 1362

  • DOI: https://doi.org/10.1126/science.1079731
  • Primary Citation of Related Structures:  
    1OAQ, 1OAR, 1OAU, 1OAX, 1OAY, 1OAZ, 1OCW

  • PubMed Abstract: 

    A single antibody was shown to adopt different binding-site conformations and thereby bind unrelated antigens. Analysis by both x-ray crystallography and pre-steady-state kinetics revealed an equilibrium between different preexisting isomers, one of which possessed a promiscuous, low-affinity binding site for aromatic ligands, including the immunizing hapten. A subsequent induced-fit isomerization led to high-affinity complexes with a deep and narrow binding site. A protein antigen identified by repertoire selection made use of an unrelated antibody isomer with a wide, shallow binding site. Conformational diversity, whereby one sequence adopts multiple structures and multiple functions, can increase the effective size of the antibody repertoire but may also lead to autoimmunity and allergy.

    • Organizational Affiliation: 

    Centre for Protein Engineering, Medical Research Council Centre, Hills Road, Cambridge CB2 2HQ, UK.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
THIOREDOXIN 1
A, B
123Escherichia coliMutation(s): 0 
UniProt
Find proteins for P0AA25 (Escherichia coli (strain K12))
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Go to UniProtKB:  P0AA25
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UniProt GroupP0AA25
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
IMMUNOGLOBULIN EC [auth H],
D [auth J]		122Mus musculusMutation(s): 0 
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
IMMUNOGLOBULIN EE [auth L],
F [auth N]		110Mus musculusMutation(s): 0 
UniProt
Find proteins for P01724 (Mus musculus)
Explore P01724 
Go to UniProtKB:  P01724
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UniProt GroupP01724
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.78 Å
  • R-Value Free: 0.276 
  • R-Value Work: 0.208 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 79.352α = 90
b = 79.467β = 90
c = 170.763γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling
AMoREphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-01-15
    Type: Initial release
  • Version 1.1: 2013-10-30
    Changes: Derived calculations, Other, Source and taxonomy, Version format compliance
  • Version 1.2: 2024-11-13
    Changes: Data collection, Database references, Other, Structure summary