Fig. 2: Crystal structure of the K20-HTS-Tail/K11-HTS-Tail/KAP-1ΔN complex. | Nature Communications

Fig. 2: Crystal structure of the K20-HTS-Tail/K11-HTS-Tail/KAP-1ΔN complex.

From: A mutual co-recognition mechanism ensures the proper assembly of heterotrimeric kinesin-2 for intraflagellar transport

Fig. 2

a Illustration of the protein constructs used for crystallization. KAP-1ΔN, K20-HTS-Tail and K11-HTS-Tail form a mini-heterotrimeric complex for structural studies. b Biochemical characterization of the K20-HTS-Tail/K11-HTS-Tail/KAP-1ΔN complex by SEC-MALS. The calculated molecular weight corresponds to a hetero-trimeric state with a stoichiometry of 1:1:1 for each component. The inset shows the SDS-PAGE analysis of each component. The experiment is independently repeated three times (n = 3). Source data are provided as a Source Data file. c A ribbon diagram of the K20-HTS-Tail/K11-HTS-Tail/KAP-1ΔN complex structure. In this drawing, KLP-20, KLP-11 and KAP-1 are colored in green, pink and blue, respectively. d A rainbow-colored diagram of the KAP-1ΔN structure, with a gradient transitioning from blue at the N-terminus to red at the C-terminus. KAP-1ΔN is composed of N-terminal helices (NTH, α1 and α2), eleven helix-based ARM-repeats (ARM1 to ARM11, α3 to α35) and C-terminal helices (CTH, α36 and α37). e, f A combined surface and ribbon diagram of the K20-HTS-Tail/K11-HTS-Tail/KAP-1ΔN complex.

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