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. 2013 Nov 25;289(2):895–908. doi: 10.1074/jbc.M113.507913

FIGURE 4.

FIGURE 4.

Lysine 362 and alanine 364 of β-tubulin change the conformation of the LRRK2 binding site. A, modeling shows the LRRK2 and taxol binding sites are in close proximity at the luminal surface of MTs. B, magnification of the area indicated in A. C-E, modeling of the structural influence of Lys-362 and Ala-364 versus Ser-362 and Ser-364 on the accessibility of the LRRK2 binding site. C, Ala-364 in TUBB and TUBB4 is unlikely to form hydrogen bonds with arginine 318 allowing for good accessibility of Lys-362 at the MT surface. D, by contrast, Ser-364 is predicted to form a hydrogen bond with arginine 318 restricting Lys-362 conformation. E, the shorter side chain of Ser-362 in comparison to Lys-362 at the MT surface is predicted to be unable to coordinate LRRK2 binding. A and B are derived from the crystal structure of bovine α/β-tubulin dimers bound to taxol; C–E are derived from the crystal structure of unbound porcine α/β-tubulin dimers.