Fig. 1: A β-hairpin motif predicted in the tail of kinesin-2 in diverse eukaryotes.
From: Regulation of kinesin-2 motility by its β-hairpin motif
a, Top, sequence diagrams of human kinesin-2 Kif3A and Kif3B. Bottom, AlphaFold3 model of the C-terminal coiled-coil region and β-hairpin motif, with the negatively charged residues at its apex shown in stick representation. The full AlphaFold3 model with pLDDT and PAE scores is shown in Extended Data Fig. 1. b, Structure-based sequence alignment of kinesin-2s from different eukaryotic supergroups. Negatively charged residues at the apex of the β-hairpin are shown in red. Conserved aromatic residues in the –3 and +4 positions relative to the apex are shown in bold. c, Aligned AlphaFold3 models of the β-hairpin in different kinesin-2s, colored as in b. d, AlphaFold3 models of homodimeric kinesin-2 Kif17 and OSM-3, which both feature an additional loop between the coiled coil and short α-helix preceding the β-hairpin. e, Size-exclusion chromatogram of reconstituted Kif3AB heterodimer with schematic of the construct inset. a.u., arbitrary units. f, SDS–PAGE of peak size-exclusion chromatography fraction after labeling SNAP-tagged Kif3A with the Alexa Fluor 647 fluorophore. g, Mass photometry of purified Kif3AB. The main peak (174 ± 15 kDa, mean ± s.d.) is consistent with the Kif3AB heterodimer mass (166 kDa).
