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. Author manuscript; available in PMC: 2022 Nov 28.
Published in final edited form as: Nat Chem Biol. 2022 Jun 20;18(8):859–868. doi: 10.1038/s41589-022-01049-9

Extended Data Fig. 4 ∣. Ligand independence of the interaction between hpMR1 and TAPBPR by native gel shift assay.

Extended Data Fig. 4 ∣

a, Native gel shift analysis for empty hpMR1/bβ2m/TAPBPR and empty MHC-I/TAPBPR complex formation. Each lane is loaded with free TAPBPR, free UVirrad/MHC-I, free empty hpMR1/bβ2m, or 1:1 molar ratio mixture with TAPBPR. Asterisk (*) denote complex formation. b, Native gel shift analysis where each lane is loaded with free TAPBPR, free hpMR1/bβ2m without (empty) or with ligands, or 1:1 mixtures with TAPBPR. Ligand/hpMR1 complexes were prepared by in vitro refolding as described in the main text. c, Quantification of the % of hpMR1/bβ2m/TAPBPR complexes formed in the presence of different ligands, relative to the free MR1 band, based on native gel electrophoresis and band quantification using ImageJ. Data are mean ± SD for n = 3 technical replicates.