Glithero, Ann, Tormo, Jose, Doering, Klaus, Kojima, Mayumi, Jones, E. Yvonne and Elliott, Tim
The crystal structure Of H-2Db complexed with a partial peptide epitope suggests an MHC class I assembly-intermediate
The Journal of Biological Chemistry, 281, (18), . (doi:10.1074/jbc.M511683200).
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In the absence of bound peptide ligands, MHC class I molecules are unstable. In an attempt to determine the minimum requirement for peptide-dependent MHC class I stabilisation we have used short synthetic peptides derived from the Sendai Virus Nucleoprotein (NP) epitope (residues 324-332 1FAPGNYPAL9) to promote its folding in vitro of H-2Db. We found that H-2Db can be stabilised 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 crystallised the complex of the H-2Db 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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