Figure 6.
Figure 6 Identification of putative macromolecular interaction
surfaces. (A) Ribbon diagram of the RNP domain in green with the
side chains of mutated residues in pink (see Figure 2C).
Residues that are essential for CTE binding are boxed. (B)
Surface representation of the RNP domain in a similar
orientation to (A). The surface is colored according to
electrostatic potential, with blue indicating positively charged
areas and red indicating negatively charged areas. (C) Structure
of the LRR domain viewed towards the convex -helical
surface. Residues at this surface that have been mutated are
shown in pink (see Figure 3E). The molecule has been rotated
180° with respect to the view in Figure 3A. (D)
Electrostatic surface of the convex outer surface of the LRR
domain viewed as in (A), and colored as in (B). Residues whose
function is discussed in the text are labeled, and boxed when
essential.
-helical
surface. Residues at this surface that have been mutated are
shown in pink (see Figure 3E). The molecule has been rotated
180° with respect to the view in Figure 3A. (D)
Electrostatic surface of the convex outer surface of the LRR
domain viewed as in (A), and colored as in (B). Residues whose
function is discussed in the text are labeled, and boxed when
essential.