Fig. 2: Structure of the multivalent MHC I chaperone network in the PLC.
From: Molecular basis of MHC I quality control in the peptide loading complex
a Cryo-EM structure of the peptide-receptive MHC I stabilized by a multivalent chaperone network in the PLC editing module (side and top view). The glycan trees of MHC I and tapasin are shown as space-filling model and stick model, respectively. Each subunit is colored separately (β2m, green; calreticulin, yellow; ERp57, red; MHC I hc, teal; tapasin, orange). The position of the second editing module is indicated in light grey. b Interaction of the MHC I glycan with the lectin domain of calreticulin. The cryo-EM map of the glycan is depicted as a transparent isosurface (contour level: 0.19, light grey). c Tapasin editing loop and interactions with the MHC I hc molecule. The cryo-EM map of the editing loop is depicted as transparent isosurface (contour level: 0.19, light grey). d β-hairpin of tapasin and interactions with β2m and MHC I hc. e Superposition of peptide-loaded MHC I (khaki, HLA-A*03:01, PDB ID: 3RL1) with the empty MHC I of the PLC (side view, including the interface with tapasin). f Superposition of PLC-associated peptide-receptive MHC I with peptide-loaded MHC I (khaki, HLA-A*03:01, PDB ID: 3RL1). Source data is available at EMDB (EMD-14119) and PDB (7QPD).
