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Insights into MHC Class I Peptide Loading from the Structure of the Tapasin-ERp57 Thiol Oxidoreductase Heterodimer
Open accessAbstract
SUMMARY Tapasin is a glycoprotein critical for loading Major Histocompatibility Complex (MHC) class I molecules with high affinity peptides. It functions within the multimeric peptide-loading complex (PLC) as a disulfide-linked, stable heterodimer with the thiol oxidoreductase ERp57, and this covalent interaction is required to support optimal PLC activity. Here we present the 2.6 Å resolution structure of the tapasin/ERp57 core of the PLC. The structure reveals the basis for the stable dimerization of tapasin and ERp57 and provides the first example of a protein disulfide isomerase family member interacting with a substrate. Mutational analysis identified a conserved surface on tapasin that interacts with MHC class I molecules and is critical for the peptide loading and editing function of the tapasin-ERp57 heterodimer. By combining the tapasin/ERp57 structure with those of other defined PLC components we present a molecular model that illuminates the processes involved in MHC class I peptide loading.
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Metadata
- Authors
- Dong, G., Wearsch, P. A., Peaper, D. R., Cresswell, P., & Reinisch, K. M.
- Venue
- Immunity
- Publisher
- Elsevier BV
- Published
- 2009-01
- Volume
- 30
- Issue
- 1
- Pages
- 21-32
- ISSN
- 1074-7613 (ISSN-L)
- OpenAlex
- W1974746017
- Cited by
- 293
- References
- 4
- FWCI
- 10.80
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Dong, G., Wearsch, P. A., Peaper, D. R., Cresswell, P., & Reinisch, K. M. (2009). Insights into MHC Class I Peptide Loading from the Structure of the Tapasin-ERp57 Thiol Oxidoreductase Heterodimer. Immunity. https://doi.org/10.1016/j.immuni.2008.10.018
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