Abstract
PURIFIED major histocompatibility complex (MHC) class I molecules have been studied at high resolution by X-ray crystallography1; the structure is a complex of a single heavy chain, β2-microglobulin light chain and a tightly bound peptide moiety. We show here that complete MHC class I molecules are post-translationally assembled into tetramers (made up of four heavy chains and four β2-microglobulin units) and that this tetrameric species is expressed on the cell surface. The multivalent tetrameric structure of class I molecules can be reconciled with models of T-cell activation that invoke antigen-receptor crosslinking, as opposed to models that depend on an allosteric change.
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Krishna, S., Benaroch, P. & Pillai, S. Tetrameric cell-surface MHC class I molecules. Nature 357, 164–167 (1992). https://doi.org/10.1038/357164a0
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DOI: https://doi.org/10.1038/357164a0
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