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 LC8 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.

Upon ctp binding, the disordered sw polypeptide attains increased helical secondary structure in a region containing a predicted coiled-coil domain.

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

From overlapping sw constructs, the authors infer residues 114-143 of sw as the binding site for ctp.

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

swa and sw bind the same groove in ctp, and are unlikely to bind ctp simultaneously.

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 ctp (dynein light chain).