Fig. 5: Structural basis for Kif3 autoinhibition.
From: Regulation of kinesin-2 motility by its β-hairpin motif
a, Close-up of the AlphaFold3 model of the autoinhibitory Kif3AB interface in cartoon representation, colored as in previous figures. Key features are labeled. The negative-stain EM class average from Fig. 4d is shown in the inset. b, Open-book representation of binding the interface between the Kif3A motor domain and Kif3A β-hairpin and coiled coil in the AlphaFold3 model. The model is shown in surface representation and colored by electrostatic potential with key residues annotated. Note the complementary charges between motor domain (positively charged; blue) and β-hairpin and coiled coil (negatively charged; red). c, Open-book representation of the binding interface between Kif3B motor domain and Kif3B β-hairpin and coiled coil. d, Schematic of kinesin-2 autoinhibition. The Kif3AB motor domains fold back to interact with β-hairpin motifs and the C-terminal coiled coil, occluding the tubulin-binding surface of each motor. Kap3 binds C-terminal regions of Kif3AB and does not relieve autoinhibition, remaining available to bind other factors that might activate Kif3. e, Example kymographs of Kif3ABWT and Kif3ABCC-mut (Kif3A-E559K D562K E556K; Kif3B-D554K D557K E561K). The gels show purified Kif3ABCC-mut. Motility parameters are provided in Extended Data Table 1.
