ERp57 interacts with conserved cysteine residues in the MHC class I peptide-binding groove |
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Authors: | Antoniou Antony N Santos Susana G Campbell Elaine C Lynch Sarah Arosa Fernando A Powis Simon J |
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Institution: | Cancer Sciences Division, University of Southampton School of Medicine, Southampton SO16 6YD, UK. |
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Abstract: | The oxidoreductase ERp57 is a component of the major histocompatibility complex (MHC) class I peptide-loading complex. ERp57 can interact directly with MHC class I molecules, however, little is known about which of the cysteine residues within the MHC class I molecule are relevant to this interaction. MHC class I molecules possess conserved disulfide bonds between cysteines 101-164, and 203-259 in the peptide-binding and alpha3 domain, respectively. By studying a series of mutants of these conserved residues, we demonstrate that ERp57 predominantly associates with cysteine residues in the peptide-binding domain, thus indicating ERp57 has direct access to the peptide-binding groove of MHC class I molecules during assembly. |
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Keywords: | PDI protein disulfide isomerase MHC major histocompatibility complex PLC peptide-loading complex |
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