Fig. 4.
Comparison of CAP-Gly-binding sites for zinc knuckle domains, the tubulin and EB1 tail peptides. (a) Zinc knuckle-induced chemical shift changes mapped on the molecular surface of the CAP-Gly-2 domain. The α-tubulin peptide is shown for comparison. Residues whose signal intensities were strongly reduced, such that (Iref − Iper)/Iref > 0.95, are shown in red, >0.90 in yellow, and >0.85 in magenta, where Iref and Iper represent the signal intensity of the reference and perturbed spectrum, respectively. The orientation of the molecule is identical with that of Fig. 1. (b) The EB1 peptide (magenta lines) bound to the p150Glued CAP-Gly domain (gray ribbons with magenta side chains) in the crystal structure (2HL3). (c) The EB1 peptide bound to the p150Glued CAP-Gly domain is compared with the NMR structure of the α-tubulin peptide (cyan/green) bound to the CLIP-170 CAP-Gly-2 domain (blue) with 20 ensemble structures.