A peptide that antagonizes TCR-mediated reactions with both syngeneic and allogeneic agonists: Functional and structural aspects

作者:Rudolph MG*; Shen LQ; Lamontagne SA; Luz JG; Delaney JR; Ge Q; Cho BK; Palliser D; McKinley CA; Chen JZ; Wilson IA; Eisen HN
来源:The Journal of Immunology, 2004, 172(5): 2994-3002.

摘要

We identify and consider some characteristics of a peptide antagonist for the Ag-specific receptor on 2C cells (the 2C TCR). The peptide, GNYSFYAL (called GNY), binds to H-2K(b), and a very high-resolution crystal structure of the GNY-K-b lex at 1.35 Angstrom is described. Although the GNY peptide does not bind to L-d, the potency of GNY-K-b as an antagonist is evident from its ability to specifically inhibit 2C TCR-mediated reactions to an allogenic agonist complex (QLSPFPFDL-L-d), as well as to a syngeneic agonist complex (SIYRYYGL-K-b). The crystal structure and the activities of alanine-substituted peptide variants point to the properties of the peptide P4 side chain and the conformation of the Tyr-P6 side chain as the structural determinants of GNYS FYAL antagonist activity.

  • 出版日期2004-3-1
  • 单位MIT