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J Biol Chem, Vol. 274, Issue 6, 3622-3631, February 5, 1999

T Cell Recognition of Hapten
ANATOMY OF T CELL RECEPTOR BINDING OF A H-2K^d-ASSOCIATED PHOTOREACTIVE PEPTIDE DERIVATIVE

Benedikt Kessler, Olivier Michielin^§, Christopher L. Blanchard, Irina Apostolou^¶, Christaiane Delarbre^¶, Gabriel Gachelin^¶, Claude Grégoire, Bernard Malissen, Jean-Charles Cerottini, Florian Wurm^**, Martin Karplus^§, and Immanuel F. Luescher

From the  Ludwig Institute for Cancer Research, Lausanne Branch, University of Lausanne, 1066 Epalinges, Switzerland, the ^¶ Department of Immunology, INSERM U277, Pasteur Institute, 75015 Paris, France,  Centre d'Immunologie, INSERM/CNRS, 13288 Marseille-Luminy, France, ^§ Institut Le Bel, Louis Pasteur University, 67404 Strasbourg, France, and ^** Centre for Biotechnology, Department of Chemistry EPFL, 1015 Lausanne, Switzerland

To elucidate the structural basis of T cell recognition of hapten-modified antigenic peptides, we studied the interaction of the T1 T cell antigen receptor (TCR) with its ligand, the H-2K^d-bound Plasmodium berghei circumsporozoite peptide 252-260 (SYIPSAEKI) containing photoreactive 4-azidobenzoic acid (ABA) on P. berghei circumsporozoite Lys²⁵⁹. The photoaffinity-labeled TCR residue(s) were mapped as Tyr⁴⁸ and/or Tyr⁵⁰ of complementary determining region 2 (CDR2). Other TCR-ligand contacts were identified by mutational analysis. Molecular modeling, based on crystallographic coordinates of closely related TCR and major histocompatibility complex I molecules, indicated that ABA binds strongly and specifically in a cavity between CDR3 and CDR2. We conclude that TCR expressing selective V and CDR3 sequences form a binding domain between CDR3 and CDR2 that can accommodate nonpeptidic moieties conjugated at the C-terminal portion of peptides binding to major histocompatibility complex (MHC) encoded proteins.

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