Chemical cross-linking of class I molecules on cells creates receptive peptide binding sites. |
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Authors: | K L Rock L Rothstein S Gamble C Gramm B Benacerraf |
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Affiliation: | Division of Lymphocyte Biology, Dana Farber Cancer Institute, Boston, MA 02115. |
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Abstract: | Class I heterodimers on the surface of cells are generally unreceptive to binding peptides in the absence of exogenous beta 2-microglobulin. Paraformaldehyde covalently cross-links beta 2-microglobulin to class I heavy chains in situ and stabilizes empty class I heterodimers. Functionally, this cross-linking creates receptive class I peptide binding sites by acting on beta 2-microglobulin-associated molecules. The presentation of preexisting peptide-class I complexes is also enhanced. These findings support a model whereby a structural alteration, the dissociation of beta 2-microglobulin, limits the existence of receptive class I molecules on normal cells and may control the half-life of active class I molecules. |
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