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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.","bibjson":{"author":[{"initials":"A","lastname":"Glithero","name":"Glithero A"},{"initials":"J","lastname":"Tormo","name":"Tormo J"},{"initials":"K","lastname":"Doering","name":"Doering K"},{"initials":"M","lastname":"Kojima","name":"Kojima M"},{"initials":"EY","lastname":"Jones","name":"Jones EY"},{"initials":"T","lastname":"Elliott","name":"Elliott T"}],"identifier":[{"id":"10.1074/jbc.m511683200","type":"doi"},{"id":"16478731","type":"pubmed"}],"issue":["18"],"journal":{"iso_abbreviation":"J. Biol. 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