Structural analysis of TCR-ligand interactions studied on H-2Kd-restricted cloned CTL specific for a photoreactive peptide derivative

Immanuel F. Luescher, Fablenne Anjuère, Manuel C. Peitsch, C. Victor Jongeneel, Jean Charles Cerottini, Pedro Romero

Research output: Contribution to journalArticlepeer-review


To study the interaction of the TCR with its ligand, the complex of a MHC molecule and an antigenic peptide, we modified a TCR contact residue of a H-2Kd-restricted antigenic peptide with photoreactive 4-azidobenzoic acid. The photoreactive group was a critical component of the epitope recognized by CTL clones derived from mice immunized with such a peptide derivative. The majority of these clones expressed Vβ1-encoded β chains that were paired with JαTA28-encoded α chains. For one of these TCR, the photoafflnlty labeled sites were mapped on the a chain as a JαTA28-encoded tryptophan and on the β chain as a residue of the C′ strand of Vβ1. Molecular modeling of this TCR suggested the presence of a hydrophobic pocket that harbors this tryptophan as well as a tyrosine on the C′ strand of Vβ1 between which the photoreactive side chain inserts. It Is concluded that this avid binding principle may account for the preferential selection of Vβ1 and JαTA28-encoded TCR.

Original languageEnglish (US)
Pages (from-to)51-63
Number of pages13
Issue number1
StatePublished - Jul 1995

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Infectious Diseases


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