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Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical.

Ding YH, Baker BM, Garboczi DN, Biddison WE, Wiley DC
Immunity 11 45-56 (1999)
Related entries: 1ao7, 1qrn, 1qsf

Cited: 263 times
EuropePMC logo PMID: 10435578

Abstract

The interactions of three singly substituted peptide variants of the HTLV-1 Tax peptide bound to HLA-A2 with the A6 T cell receptor have been studied using T cell assays, kinetic and thermodynamic measurements, and X-ray crystallography. The three peptide/MHC ligands include weak agonists and antagonists with different affinities for TCR. The three-dimensional structures of the three A6-TCR/peptide/HLA-A2 complexes are remarkably similar to each other and to the wild-type agonist complex, with minor adjustments at the interface to accommodate the peptide substitutions (P6A, V7R, and Y8A). The lack of correlation between structural changes and the type of T cell signals induced provides direct evidence that different signals are not generated by different ligand-induced conformational changes in the alphabeta TCR.

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Related citations provided by authors (2)

  1. Structure of the complex between human T-cell receptor, viral peptide and HLA-A2.. Garboczi DN, Ghosh P, Utz U, Fan QR, Biddison WE, Wiley DC Nature 384 134-41 (1996)
  2. Two human T cell receptors bind in a similar diagonal mode to the HLA-A2/Tax peptide complex using different TCR amino acids.. Ding YH, Smith K, Garboczi DN, Utz U, Biddison WE, Wiley DC Immunity 8 403-411 (1998)

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