Fig. 3: Role of Grp94F199A for Grp94 loading conformation with HSP990. | Nature Communications

Fig. 3: Role of Grp94F199A for Grp94 loading conformation with HSP990.

From: Mechanism of client loading from BiP to Grp94 and its disruption by select inhibitors

Fig. 3

A Normalized Grp94 bulk FRET efficiency changes at 8 μM BiP NBD for wild-type Grp94, Grp94L163A, and Grp94F199A with no inhibitor or 50 μM inhibitor. Data points are from independent replicate measurements. See Supplementary Fig. 2 and 10 for complete BiP concentration series. B smFRET efficiency histograms for Grp94F199A in the presence of 50 μM HSP990. C Overlay of smFRET histograms for wild-type Grp94 (blue dashed represents outline of histogram from the lower panel of Fig. 2C) and Grp94F199A (gray bars) in the presence of 50 μM HSP990 and 8 μM BiP NBD. Count values on left and right x-axes are for wild-type Grp94 and Grp94F199A, respectively. Source data are provided as a Source Data file.

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