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. Author manuscript; available in PMC: 2010 Jun 10.
Published in final edited form as: Structure. 2009 Jun 10;17(6):833–842. doi: 10.1016/j.str.2009.04.010

Figure 5. Structural Constraints and Alterations Provoked by the Vinculin-Raver1 Interaction.

Figure 5

(A) Superposition of the Vt:RRM1-3 complex (color coding is the same as in Figure 3) with full-length, inactive human vinculin (shown in pink). The raver1 binding site is occluded by the 882-890 loop region of inactive vinculin. Asp882 of Vt in its raver1 bound state is indicated as well as Pro877 of inactive vinculin (dashed arrows).

(B) Interaction with vinculin alters the structure of the binding loops of raver1. Superposition of the native mouse RRM1 domain (PDBID 1WI6, yellow) onto human RRM1 (blue) when bound to vinculin (green). Upon binding to vinculin, β-strand β4 moves as indicated by red arrows. In the unbound raver1 structure, only two interactions are found between the β-hairpin and the loop region situated between strand β1 and helix α1 (Arg127 and Asp77 as well as Arg129 and Leu74; not shown for clarity). However, in the Vt:raver1 complex the side chain of Arg121 interacts with main chain oxygen of Arg119; the side chain of Arg119 engages in electrostatic interactions with the side chains of Asp69 and Glu74; and the side chain of Arg117 is in contact with the main chain oxygen of Glu120. The hydrophobic cavity observed on the surface near the β-hairpin is rather large in the unbound conformation, which almost completely disappears in the complex.