The Crystal Structure of H-2D super(b) Complexed with a Partial Peptide Epitope Suggests a Major Histocompatibility Complex Class I Assembly Intermediate

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 epitop...

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Published inThe Journal of biological chemistry Vol. 281; no. 18; pp. 12699 - 12704
Main Authors Glithero, Ann, Tormo, Jose, Doering, Klaus, Kojima, Mayumi, Jones, EYvonne, Elliott, Tim
Format Journal Article
LanguageEnglish
Published 05.05.2006
Subjects
Sendai virus
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Summary: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, super(1)FAPGNYPAL super(9)) to promote its folding in vitro of H-2D super(b). We found that H-2D super(b) can be stabilized by the pentapeptide super(5)NYPAL super(9), 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 super(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.
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ISSN:0021-9258
1083-351X