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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.

Original publication

DOI

10.1002/eji.1830221214

Type

Journal article

Journal

Eur J Immunol

Publication Date

12/1992

Volume

22

Pages

3121 - 3125

Keywords

Amino Acid Sequence, Animals, Epitopes, Histocompatibility Antigens Class I, Mice, Molecular Sequence Data, Peptide Fragments, Protein Conformation