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. Author manuscript; available in PMC: 2017 Apr 1.
Published in final edited form as: J Neurochem. 2016 Mar 15;137(2):287–298. doi: 10.1111/jnc.13557

Figure 2. 3D structure of gp120 and TUBB3.

Figure 2

The tridimensional structures of gp120 (A and B) show that two helices in gp120 (Helix-A in purple and Helix-B in yellow) occupied two opposite sides and both could be contributing to the effective binding to the CTT (C, light blue) of TUBB3. Furthermore, we indicated the lysine residues present in Helix-A that could be responsible in the stabilization of helix-helix interaction between Helix-A and CTT. D. BiacoreT200 was used to determine the kinetic parameters for the binding of recombinant TUBB3, tubulin dimer, and assembled MTs Helix-A and HeliX-B peptides. Peptides were injected at different concentrations (10 nM – 500 µM). Data are from three independent experiments.