Role of 2C T Cell Receptor Residues in the Binding of Self- and Allo-Major Histocompatibility Complexes

doi:10.1084/jem.191.8.1355

Published online 18 April 2000.

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© The Rockefeller University Press, 0022-1007/2000/4/1355/ $5.00
The Journal of Experimental Medicine, Volume 191, Number 8, April 17, 2000 1355-1364

Original Article

Role of 2C T Cell Receptor Residues in the Binding of Self– and Allo–Major Histocompatibility Complexes

Peter U.Y. Lee^a, Hywyn R.O. Churchill^a, Mark Daniels^b, Stephen C. Jameson^b, and David M. Kranz^a
^a Department of Biochemistry, University of Illinois, Urbana, Illinois 61801
^b Department of Laboratory Medicine and Pathology and the Center for Immunology, University of Minnesota Medical School, Minneapolis, Minnesota 55455

Correspondence to: David M. Kranz, Department of Biochemistry, University of Illinois, 600 S. Mathews, Urbana, IL 61801. Tel:217-244-2821 Fax:217-244-5858 E-mail:d-kranz{at}uiuc.edu.

T cell clone 2C recognizes the alloantigen L^d and the positiveselecting major histocompatibility complex (MHC), K^b. To explorethe molecular basis of T cell antigen receptor (TCR) bindingto different peptide/MHC (pMHC) complexes, we performed alaninescanning mutagenesis of the 2C TCR. The TCR energy maps forQL9/L^d and SIYR/K^b were remarkably similar, in that 16 of 41V ${alpha}$ and Vß alanine mutants showed reduced binding to bothligands. Several TCR residues varied in the magnitude of energycontributed to binding the two ligands, indicating that thereare also unique interactions. Residues in complementarity determiningregion 3 ${alpha}$ showed the most notable differences in binding energeticsamong the ligands QL9/L^d, SIYR/K^b, and the clonotypic antibody1B2. Various lines of evidence suggest that these differencesrelate to the mobility of this loop and point to the key roleof conformational dynamics in pMHC recognition.

Key Words: T cell receptor, peptide–major histocompatibility complex,complementarity determining region, alloantigen, antigen recognition

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