Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey produced as a recombinant fusion protein in bacterial system.

Mixture of purified sw and Dlc90F induces changes in the secondary structure of these proteins. The unordered sw polypeptide attains more helical structure.

Changes in secondary structure upon mixing of proteins was monitored by circular dichroism.

Interaction in vitro; proteins produced as a recombinant fusion proteins in bacterial system.

Gel filtration chromatography indicates that sw, ctp, robl and Dlc90F form a 112 kDa Dynein regulatory complex of 2:2:2:2 stoichiometry.

Interaction in vitro; proteins produced as a recombinant fusion proteins in bacterial system.

sw can bind to ctp and Dlc90F simultaneously, as judged by the apparent molecular weight of complexes on gel filtration columns.

Interaction in vitro; proteins produced as a recombinant fusion proteins in bacterial system.

sw can bind to ctp and Dlc90F simultaneously.

The light chain binding site of sw (dynein intermediate chain) remains structurally disordered upon binding to Dlc90F (dynein light chain).