Fig. 4: Structural basis for the docking of axonemal dyneins to the doublet microtubule surface. | Nature Communications

Fig. 4: Structural basis for the docking of axonemal dyneins to the doublet microtubule surface.

From: Structure of a microtubule-bound axonemal dynein

Fig. 4

a The ODA docking complex (ODA-DC) is a heterotrimer consisting of a DC1/DC2 coiled-coil and a globular DC3 subunit that repeats every 24 nm. Each ODA complex interacts with one copy of DC1/DC2 coiled-coil, and the DC3 subunit from the proximal ODA-DC. Thus, each ODA-DC contributes to the binding of two ODA complexes. b Atomic model of the interactions between the ODA and the ODA-DC. The C terminus of the DC1/DC2 coiled-coil interacts with the tail domains of β- and γ-HC. DC3 interacts with helical bundle 3 of the γ-HC tail. NDD N-terminal dimerization domain.

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