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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 A) 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, DeltaTm = 16 degrees 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.","bibjson":{"author":[{"initials":"AR","lastname":"Khan","name":"Khan AR"},{"initials":"BM","lastname":"Baker","name":"Baker BM"},{"initials":"P","lastname":"Ghosh","name":"Ghosh P"},{"initials":"WE","lastname":"Biddison","name":"Biddison WE"},{"initials":"DC","lastname":"Wiley","name":"Wiley DC"}],"identifier":[{"id":"10.4049/jimmunol.164.12.6398","type":"doi"},{"id":"10843695","type":"pubmed"}],"issue":["12"],"journal":{"iso_abbreviation":"J. 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