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*
Department of Genetics, Washington University School of Medicine, St. Louis, MO 63110;
Department of Microbiology, University of South Dakota School of Medicine, Vermillion, SD 57069
Before peptide binding, a variety of endoplasmic reticulum (ER)
proteins are associated with class I including calnexin, TAP,
calreticulin, and tapasin. Although the selective functions of any one
of these ER proteins have been difficult to define, individually or in
combination they perform two general chaperone functions for class I.
They promote assembly of the class I heterotrimeric molecule (heavy (H)
chain, ß2m, and peptide) and they retain
incompletely assembled complexes in the ER. In this study, we present
evidence that calreticulin clearly differs from calnexin in how it
associates with class I. Regarding the structural basis of the
association, the oligosaccharide moiety in the 
1 domain and the
amino acid residue at position 227 in the 3 domain were both found
to be critical for the interaction of class I with calreticulin.
Interestingly, calreticulin displayed sensitivity to class I peptide
binding even in TAP-deficient human or mouse cells. Thus, calreticulin
is clearly more specific than calnexin in the structures and
conformation of the class I molecule with which it can interact.
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