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. Author manuscript; available in PMC: 2015 Oct 7.
Published in final edited form as: Structure. 2014 Sep 18;22(10):1520–1527. doi: 10.1016/j.str.2014.08.009

Figure 3. Residue conservation analysis of CTL2.

Figure 3

(A) Surface representation of the WT CTL2 domain (marine blue) is oriented in similar fashion to the one displayed in Figure 2 (left side). The N and C terminus are labeled, with the residues colored in light gray. (B) Surface conservation representation from the closest Piezo homologs as calculated by ProFunc (Laskowski et al., 2005a, b) and displayed on the WT CTL2 domain structure. (C) Surface conservation representation from representative Piezo homologs taken from broad branches of eukaryotic kingdom (Fig S1) as calculated by ConSurf (Ashkenazy et al., 2010). The left panels of B and C show the surface of CTL2 upon ~+90° rotation along the y-axis from the view in A, dominated by the solvent exposed surface of sheet 1, while the right panel shows the surface of CTL2 upon -90° rotation from A (180° from the left panels). Surface conservation is colored in a rainbow gradient scheme in such a way that the least conserved region is colored in blue and the most conserved region is colored in red. M31R is located at the conserved sheet 1 surface of CTL2 displayed in the left panels. See also Figures S2 and S4.