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The nature of the MHC class I peptide loading complex
Author(s) -
Cresswell Peter,
Bangia Naveen,
Dick Tobias,
Diedrich Gundo
Publication year - 1999
Publication title -
immunological reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.839
H-Index - 223
eISSN - 1600-065X
pISSN - 0105-2896
DOI - 10.1111/j.1600-065x.1999.tb01353.x
Subject(s) - transporter associated with antigen processing , calreticulin , mhc class i , major histocompatibility complex , biology , antigen processing , cd74 , mhc restriction , endoplasmic reticulum , antigen presentation , chaperone (clinical) , calnexin , microbiology and biotechnology , beta 2 microglobulin , peptide , biochemistry , antigen , genetics , immunology , cytotoxic t cell , in vitro , medicine , pathology
Summary: Peptide binding to major histocompatibility complex (MHC) dass I molecules occurs in the endoplasmic reticulum (ER). Efficient peptide binding requires a number of components in addition co the MHC class I‐β 2 microglobulin dimer (β 2 m). These include the two subunits of the transporter associated with antigen presentation (TAP1 and TAP2), which are essential for introducing peptides into the ER from the cytosol, and tapasin, an MHC‐encoded membrane protein. Prior to peptide binding, MHC class I‐β 2 m dimers form part of a large multisubnnit ER complex which includes TAP and tapasin. In addition to these specialized components two soluble ‘house‐keeping’ proteins, the chaperone calreticulin and the thiol oxidoreductase ERp57, are also components of this complex. Our current understanding of the nature and function of the MHC class I peptide loading complex is the topic of this review.