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*
Department of Molecular and Cellular Biology and
Howard Hughes Medical Institute, Harvard University, Cambridge MA 02138;
Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla, CA 92093; and
§
Molecular Immunology Section, Neuroimmunology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda MD 20892
The crystal structure of the human class I MHC molecule HLA-A2
complexed with of an octameric peptide, Tax8 (LFGYPVYV), from human T
cell lymphotrophic virus-1 (HTLV-1) has been determined. This structure
is compared with a newly refined, higher resolution (1.8 Å) structure
of HLA-A2 complexed with the nonameric Tax9 peptide (LLFGYPVYV) with
one more N-terminal residue. Despite the absence of a peptide residue
(P1) bound in the conserved N-terminal peptide-binding pocket of the
Tax8/HLA-A2 complex, the structures of the two complexes are
essentially identical. Water molecules in the Tax8 complex replace the
terminal amino group of the Tax9 peptide and mediate a network of
hydrogen bonds among the secondary structural elements at that end of
the peptide-binding groove. Thermal denaturation measurements indicate
that the Tax8 complex is much less stable,
Tm = 16°C, than the Tax9 complex,
but both can sensitize target cells for lysis by some Tax-specific CTL
from HTLV-1 infected individuals. The absence of a P1 peptide residue
is thus not enough to prevent formation of a "closed conformation"
of the peptide-binding site. TCR affinity measurements and cytotoxic T
cell assays indicate that the Tax8/HLA-A2 complex does not functionally
cross-react with the A6-TCR-bearing T cell clone specific for
Tax9/HLA-A2 complexes.
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