dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke protein 7 (RSP7) and similar proteins
Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules. RSP7 is a cAMP-dependent protein kinase (PKA) RII-like protein. RSP7 contains an N-terminal domain which shows high sequence similarity to the dimerization/docking (D/D) domain of regulatory subunit of PKA. The D/D domain of RSP7 heterodimerizes with the D/D domain of RSP11 to form an X-type four-helix bundle within the radial spoke RS1 complex.
Structure:7JTK: Chlamydomonas reinhardtii flagellar radial spoke protein 7 (RSP7) and RSP11 form a heterodimer within the radial spoke RS1 complex; contacts at 4A