Figure 4 - full size

 

Figure 4.
Fig. 4. Detail of key peptide binding residues (a) Comparison of the positions of active site side chains. Strands β1, β2 and β7 are shown for all molecules, with the remainder of Spred1. W28 and F86 are shown as sticks. Backbone location of selected residues is shown by white text. Colours: Spred1, red (light red outside peptide-binding groove); Enabled, blue; Homer, purple; WASP, black; nitrogen, blue (blue-grey: Spred1, cyan: Enabled); oxygen, red. Spred W28, yellow arrowhead. Homologous tryptophans, grey arrow. F86, black arrow. (b) The Spred1 strand β2 is translated in comparison to the other EVH1 domains. Strands β1, β2 and β2′ are shown all molecules, with the remainder of Spred1. Spred strand β2, black arrow; Other EVH1 strand β2, dashed arrow. Colours as in (a). (c) Comparison of Y21 equivalents in the two Spred1 structures. W28 and R/Y21 are shown as sticks. Colours as in (a), Spred1 molecule B in green. Enabled Y21, grey arrow. Spred1 R21 (two conformations), black and yellow arrows.

The above figure is reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (2005, 579, 1161-1166) copyright 2005.