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In the absence of bound peptide ligands, major histocompatibility complex (MHC) class I molecules are unstable. In an attempt to determine the minimum requirement for peptide-dependent MHC class I stabilization, we have used short synthetic peptides derived from the Sendai virus nucleoprotein epitope (residues 324-332, 1FAPGNYPAL9) to promote its folding in vitro of H-2D(b). We found that H-2D(b) can be stabilized by the pentapeptide 5NYPAL9, which is equivalent to the C-terminal portion of the optimal nonapeptide and includes both the P5 and P9 anchor residues. We have crystallized the complex of the H-2D(b) molecule with the pentamer and determined the structure to show how a quasi-stable MHC class I molecule can be formed by occupancy of a single binding pocket in the peptide-binding groove.

Original publication




Journal article


J Biol Chem

Publication Date





12699 - 12704


Animals, CHO Cells, Cricetinae, Crystallography, X-Ray, Epitopes, H-2 Antigens, Histocompatibility Antigen H-2D, Histocompatibility Antigens Class I, Humans, Ligands, Molecular Conformation, Nucleoproteins, Peptides, Protein Structure, Secondary, Sendai virus