Binding of truncated peptides to the MHC molecule IAd
- 9 December 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 294 (3) , 244-246
- https://doi.org/10.1016/0014-5793(91)81439-f
Abstract
A peptide comprising amino acids 323–339 of chicken ovalbumin is known to bind to two heterodimeric conformations of the MHC molecule IAd, and to each of its separate α- and β-chains. We report that minor C- and N-terminal truncations of the parent peptide do not alter the binding pattern. A decrease in binding activity was observed upon deletion of the histidine residues of the already truncated peptides. Peptides as short as 4 amino acids associate weakly with all four proteinsKeywords
This publication has 8 references indexed in Scilit:
- Interactions between Immunogenic Peptides and MHC ProteinsAnnual Review of Immunology, 1991
- Refolding and reassembly of separate alpha and beta chains of class II molecules of the major histocompatibility complex leads to increased peptide-binding capacity.Proceedings of the National Academy of Sciences, 1990
- Peptide binding to HLA-DR1: a peptide with most residues substituted to alanine retains MHC binding.The EMBO Journal, 1990
- Specific binding of antigenic peptides to separate alpha and beta chains of class II molecules of the major histocompatibility complex.Proceedings of the National Academy of Sciences, 1990
- Structural Intermediates in the Reactions of Antigenic Peptides with MHC MoleculesPublished by Cold Spring Harbor Laboratory ,1989
- The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigensNature, 1987
- Structural characteristics of an antigen required for its interaction with Ia and recognition by T cellsNature, 1987
- T-cell activation by peptide antigen: effect of peptide sequence and method of antigen presentation.Proceedings of the National Academy of Sciences, 1985