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J. Exp. Med.,
Volume 189, Number 2, January 18, 1999 359-370
By
From the * Department of Microbiology and Immunology, University of North Carolina at Chapel
Hill, Chapel Hill, North Carolina 27599; and the The T cell receptor (TCR), from a xeno-reactive murine cytotoxic T lymphocyte clone
AHIII12.2, recognizes murine H-2Db complexed with peptide p1027 (FAPGVFPYM), as well
as human HLA-A2.1 complexed with peptide p1049 (ALWGFFPVL). A commonly proposed model (the molecular mimicry model) used to explain TCR cross-reactivity suggests that the
molecular surfaces of the recognized complexes are similar in shape, charge, or both, in spite of
the primary sequence differences. To examine the mechanism of xeno-reactivity of AHIII12.2,
we have determined the crystal structures of A2/p1049 and Db/p1027 to 2.5 Å and 2.8 Å resolution, respectively. The crystal structures show that the TCR footprint regions of the two
class I complexes are significantly different in shape and charge. We propose that rather than
simple molecular mimicry, unpredictable arrays of common and differential contacts on the
two class I complexes are used for their recognition by the same TCR.
Laboratory of Cell Biology, National Cancer
Institute, National Institutes of Health, Bethesda, Maryland 20892
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