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. Author manuscript; available in PMC: 2014 Oct 3.
Published in final edited form as: Brain Res. 2013 Aug 12;1533:1–15. doi: 10.1016/j.brainres.2013.08.010

Figure 1.

Figure 1

Secondary structure predictions. (A) Sequence alignment of D10 (L1087-F1238, See Table 1) with domain 1 (L40-Y154), with D10 exhibiting 22% sequence identity and 41% similarity. The D1185 residue (bold and double underline) is located in the middle of the long, 34-residue segment (V1167-H1200, dotted line) that does not align with D1. Two conserved tryptophan residues found in Helices A and C are shown in grey. (B) D10Δ, excluding residues from V1167-H1200, sequence aligned with domain 1 exhibiting 29% sequence identity and 52% similarity. The high sequence homology with domain 1 allows us to predict that Helix A in D10 as residues K1092-L1114 (underlined), Helix B as residues V1126 - E1160, and Helix C as residues T1201-G1230. Also shown is the sequence alignment of D13 (L1441-F1556) with D1. The alignment shows 28% identity and 49% similarity between D13 and D1. We assigned L1445-F1467 in D13 as Helix A (underlined), V1480-A1514 as Helix B, and K1519-G1548 as Helix C. The D1478 residue (bold, and double underline) is at the end of the segment connecting Helix A and Helix B. (C) A 40-residue segment (G1161 -H1200) located between Helix B and Helix C in D10.