Fig. 6: Fine-tuning MHC-I/TAPBPR interactions through α3 domain mutants.
From: High throughput pMHC-I tetramer library production using chaperone-mediated peptide exchange
a Alignment of the α3 domain sequences from murine H-2Dd, H-2Ld and human HLA-A*02:01. Conserved residues are highlighted in yellow. The M228T mutation site is highlighted in blue. * indicates residues directly participating in TAPBPR interactions, as shown in published mutagenesis studies and crystal structures. b TAPBPR/H-2Dd α3 domain interface from PDB ID 5WER5 (left panel) and with the M228T mutation modeled (right panel). c Size exclusion chromatograms of H-2Dd M228T refolded with either high-affinity P18-I10 or goldilocks gP18-I10 peptides, with and without TAPBPR. d LC/MS analysis of the peptide region from SEC-purified gP18/H-2DdM228T and H-2DdM228T/TAPBPR peaks from (c). Data shown are representative of triplicate SEC and LC/MS experiments.
