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TitleMolecular basis of MHC I quality control in the peptide loading complex.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 4701, Year 2022
Publish dateAug 10, 2022
AuthorsAlexander Domnick / Christian Winter / Lukas Sušac / Leon Hennecke / Mario Hensen / Nicole Zitzmann / Simon Trowitzsch / Christoph Thomas / Robert Tampé /
PubMed AbstractMajor histocompatibility complex class I (MHC I) molecules are central to adaptive immunity. Their assembly, epitope selection, and antigen presentation are controlled by the MHC I glycan through a ...Major histocompatibility complex class I (MHC I) molecules are central to adaptive immunity. Their assembly, epitope selection, and antigen presentation are controlled by the MHC I glycan through a sophisticated network of chaperones and modifying enzymes. However, the mechanistic integration of the corresponding processes remains poorly understood. Here, we determine the multi-chaperone-client interaction network of the peptide loading complex (PLC) and report the PLC editing module structure by cryogenic electron microscopy at 3.7 Å resolution. Combined with epitope-proofreading studies of the PLC in near-native lipid environment, these data show that peptide-receptive MHC I molecules are stabilized by multivalent chaperone interactions including the calreticulin-engulfed mono-glucosylated MHC I glycan, which only becomes accessible for processing by α-glucosidase II upon loading of optimal epitopes. Our work reveals allosteric coupling between peptide-MHC I assembly and glycan processing. This inter-process communication defines the onset of an adaptive immune response and provides a prototypical example of the tightly coordinated events in endoplasmic reticulum quality control.
External linksNat Commun / PubMed:35948544 / PubMed Central
MethodsEM (single particle)
Resolution3.73 Å
Structure data

EMDB-14119, PDB-7qpd:
Structure of the human MHC I peptide-loading complex editing module
Method: EM (single particle) / Resolution: 3.73 Å

Source
  • homo sapiens (human)
  • human (human)
KeywordsIMMUNE SYSTEM / antigen processing / peptide proofreading / chaperones / MHC I

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