Fig. 5: Model for chaperone function of tapasin towards peptide-receptive MHC I. | Nature Communications

Fig. 5: Model for chaperone function of tapasin towards peptide-receptive MHC I.

From: Structure of an MHC I–tapasin–ERp57 editing complex defines chaperone promiscuity

Fig. 5

Schematic of molecular motions leading to stabilized peptide-receptive clients (MHC I hc, teal; β2m, green) upon association with tapasin (orange; left, side view; right, top view). Conformational changes are indicated by black arrows. The dotted line indicates a polar interaction between tapasin (Glu72) and chaperoned MHC I (Tyr84 of the heavy chain, hc). For reasons of clarity, ERp57 (red) is not shown in the right panel.

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