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. Author manuscript; available in PMC: 2009 Jul 24.
Published in final edited form as: J Biol Chem. 2006 Mar 22;281(19):13628–13635. doi: 10.1074/jbc.M513730200

Fig. 8.

Fig. 8

Location of destabilizing mutations. Mutations that interfere with β-tubulin folding are shown on the molecular structure reported by Lowe et al. (37). The β subunit is shown in magenta and a small portion of the α subunit is shown in dark blue. Regions affected by the 6H3 truncation are in cyan, the 6H2 12 amino acid deletion is in orange, the L187R substitution is in green, and the Y398C substitution is in red. The tubulin is oriented with the region that faces the interior of the microtubule to the left (In) and the region that faces the exterior to the right (Out). Helices H5, H11, and H12; and β-sheet S9 are also labeled. The structure was drawn with MacPyMol (www.pymol.org).