Extended Data Fig. 5: Binding affinity between EB1 and its binding partners was not changed by KR6Q mutation.
From: Phase separation of EB1 guides microtubule plus-end dynamics
ITC binding curves for interaction of EB1 and its binding partners upon KR6Q mutation. (a) MCAK peptide, aa 85-118; (b) TIP150 peptide, aa 823-856; (c) CLASP1 peptide, aa 713-747; (d) CLASP2 peptide, aa 490-523; (e) p150Glued CAP-GLY domain (aa 1-105). For ITC assay, the peptides and p150Glued CAP-GLY domain were used at 1 mM in syringe, while the purified EB1 wild type and KR6Q mutant were used at 50 μM in cell. Data are representative from three independent replicates. All peptide sequences were listed in Supplementary Table 1.
