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. Author manuscript; available in PMC: 2022 Jun 18.
Published in final edited form as: Curr Opin Immunol. 2021 Jun 18;70:122–128. doi: 10.1016/j.coi.2021.04.012

Figure 2.

Figure 2.

A conceptual model for chaperone recognition of the MHC-I conformational landscape. The vertical axis is free energy, and the horizontal axis shows the potential conformations that MHC-I can adopt. Unfolded or misfolded, α2 helix (denoted in red) has been shown to result in compromised TAPBPR recognition in situ [8]. However, disruption of the α1 helix does not influence TAPBPR binding [8]. MHC-I loaded with high affinity peptides may also interact with TAPBPR in an allotype-dependent manner, through the sampling of a minor, open conformation of the α2–1 helix. Introducing a disulfide linkage (Y84C/A139C) that restricts the mobility of the α2–1 helix abolishes TAPBPR binding in vitro. Figure adapted from McShan et al. (2019).