Fig. 3: Cryo-EM structure of full-length autoinhibited P-Rex1.
From: Structure of the metastatic factor P-Rex1 reveals a two-layered autoinhibitory mechanism
a, Cryo-EM map and structure of full-length P-Rex1. Map density for T4L is omitted for clarity (Extended Data Fig. 8) b, Inset, 2D classification from an equivalent molecular view for reference. c, Multiple indicated P-Rex1 views with domains highlighted. d, BS3 crosslink constraints (FDR = 6.8 %) from wild-type full-length P-Rex1 mapped onto the pipes-and-planks depiction of the full-length autoinhibited P-Rex1 model indicates numerous close range spatial constraints that are consistent with the modeled domain topology shown in a–c. Satisfied crosslinks are colored blue (<30 Å between lysine Cβ atoms), while crosslinks that exceed the maximum allowable distance (indicative of conformational flexibility) are in red (>30 Å between lysine Cβ atoms). Lysine Cβ atoms are shown as blue spheres. e, Circos plot of BS3 crosslinking mass spectrometry of full-length wild-type P-Rex1. Dashed line (black) indicates position of an IDL (located on the tip of the 4HB) removed in the cryo-EM construct.
