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Qualitative and quantitative differences in t cell receptor binding of agonist and antagonist ligands

Academic Article
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Overview

authors

  • Alam, S. M.
  • Davies, G. M.
  • Lin, C. M.
  • Zal, T.
  • Nasholds, W.
  • Jameson, S. C.
  • Hogquist, K. A.
  • Gascoigne, Nicholas
  • Travers, P. J.

publication date

  • February 1999

journal

  • Immunity  Journal

abstract

  • The kinetics of interaction between TCR and MHC-peptide show a general relationship between affinity and the biological response, but the reported kinetic differences between antigenic and antagonistic peptides are very small. Here, we show a remarkable difference in the kinetics of TCR interactions with strong agonist ligands at 37 degrees C compared to 25 degrees C. This difference is not seen with antagonist/positive selecting ligands. The interaction at 37 degrees C shows biphasic binding kinetics best described by a model of TCR dimerization. The altered kinetics greatly increase the stability of complexes with agonist ligands, accounting for the large differences in biological response compared to other ligands. Thus, there may be an allosteric, as well as a kinetic, component to the discrimination between agonists and antagonists.

subject areas

  • Animals
  • Binding Sites
  • Biosensing Techniques
  • Dimerization
  • H-2 Antigens
  • Kinetics
  • Ligands
  • Major Histocompatibility Complex
  • Ovalbumin
  • Peptide Fragments
  • Peptides
  • Receptors, Antigen, T-Cell
  • Temperature
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Identity

International Standard Serial Number (ISSN)

  • 1074-7613

Digital Object Identifier (DOI)

  • 10.1016/s1074-7613(00)80023-0

PubMed ID

  • 10072075
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Additional Document Info

start page

  • 227

end page

  • 237

volume

  • 10

issue

  • 2

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