Short peptides assist the folding of free class I heavy chains in solution.
Previous experiments have shown that short peptides coresponding to naturally processed epitopes of viral antigens can induce a conformational change in the class I heavy chain (HC) to which they bind in the fully assembled molecule. Here, we present evidence that the mechanism for this conformational change may involve binding of peptide to a partially unfolded form of free HC, followed by its subsequent folding. These results may be important for understanding the way in which class I molecules are assembled in vivo, and how certain epitopes are selected for presentation to T cells.
D000595:Amino Acid Sequence; D000818:Animals; D000939:Epitopes; D015395:Histocompatibility Antigens Class I / Q000737:chemistry* / Q000187:drug effects; D051379:Mice; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000494:pharmacology*; D011487:Protein Conformation / Q000187:drug effects
D000939:Epitopes; D015395:Histocompatibility Antigens Class I; D010446:Peptide Fragments