Recognition of core and flanking amino acids of MHC class II-bound peptides by the T cell receptor

Autor:	Eve Robinson, Lisa K. Denzin, Derek B. Sant'Angelo, Charles A. Janeway
Rok vydání:	2002
Předmět:	chemistry.chemical_classification MHC class II biology CD74 Immunology T-cell receptor chemical and pharmacologic phenomena Peptide binding Peptide MHC restriction Major histocompatibility complex chemistry Biochemistry MHC class I biology.protein Immunology and Allergy
Zdroj:	European Journal of Immunology. 32:2510-2520
ISSN:	1521-4141 0014-2980
Popis:	CD4 T cells recognize peptides bound to major histocompatibility complex (MHC) class II molecules. Most MHC class II molecules have four binding pockets occupied by amino acids 1, 4, 6, and 9 of the minimal peptide epitope, while the residues at positions 2, 3, 5, 7, and 8 are available to interact with the T cell receptor (TCR). In addition MHC class II bound peptides have flanking residues situated outside of this peptide core. Here we demonstrate that the flanking residues of the conalbumin peptide bound to I-A(k) have no effect on recognition by the D10 TCR. To study the role of peptide flanks for recognition by a second TCR, we determined the MHC and TCR contacting amino acids of the I-A(b) bound Ealpha peptide. The Ealpha peptide is shown to bind I-A(b) using four alanines as anchor residues. TCR recognition of Ealpha peptides with altered flanking residues again suggested that, in general, no specific interactions occurred with the peptide flanks. However, using an HLA-DM-mediated technique to measure peptide binding to MHC class II molecules, we found that the peptide flanking residues contribute substantially to MHC binding.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::1c0e5a55c7e109a59b84e75f8254c56b https://doi.org/10.1002/1521-4141(200209)32:9<2510::aid-immu2510>3.0.co Zobrazit plný text záznamu Plný text