![]() SSR alpha and associated calnexm are major calcium binding proteins of the endoplasmic reticulum membrane. Endoplasmic reticulum resident protein of 90 kilodaltons associates with the T-and B-cell antigen receptors and major histocompatibility complex antigens during their assembly. Hochstenbach F, David V, Watkins S et al. Participation of a novel 88-kD protein in the biogenesis of murine class I histocompatibility molecules. This process is experimental and the keywords may be updated as the learning algorithm improves.ĭegen E, Williams DB. These keywords were added by machine and not by the authors. The controversial issue of whether CNX/CRT function solely as lectins or also as “classical” chaperones that recognize the unfolded polypeptide portion of glycoproteins is presented and the evidence supporting current models is discussed in detail. Furthermore, the domain organization and locations of functional sites have been revealed through mutagenesis and the recent determination of the structure of the ER luminal domain of CNX and a portion of CRT. Mechanistic insights into how this function is accomplished have been provided through diverse approaches which include interfering with the recognition of glycoproteins through CNX/CRT’s lectin site, expression of CNX/CRT and model substrates in heterologous systems, gene disruption, and reconstitution of function with purified components in vitro. In this chapter we present the evidence that calnexin (CNX) and calreticulin (CRT) function as molecular chaperones to assist in the folding and subunit assembly of the majority of Asn-linked glycoproteins that pass through the endoplasmic reticulum. ![]()
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