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. 2010 Sep 9;19(22):4462–4473. doi: 10.1093/hmg/ddq377

Figure 5.

Figure 5.

Tubulin structure and positions of TUBB3 amino acid substitutions associated with MCD, in comparison with TUBB3 amino acid substitutions associated with CFEOM3. (A and B) Structural representation (face A) of the α-/β-heterodimer depicted with (A) or without surface delimitation (B), revealing relative positions of MCD TUBB3 amino acid substitutions either inside the monomer (p.E205K, p.A302V and p.M388V) or on the surface (p.G82R, p.T178M and p.M323V). α- and β-subunits are, respectively, represented in light and dark grey. Contrary to helices that are in grey, β-strands are visualized in dark blue. Localization of TUBB3 amino acid substitutions is summarized in (C). (D and E) Structural representation (face B) of the α-/β-heterodimer depicted with (D) or without surface delimitation (E), revealing relative positions of CFEOM3 TUBB3 amino acid substitutions either inside the heterodimer (p.R62, p.A302 and p.R380) or on the surface (p.R262, p.E410 and p.D417). These representations (A–E) show that amino acid substitutions localized on the surface are on opposite sides in case of CFEOM3 (Face B, in D and E) and MCD mutations (Face A, in A and B).