dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke protein 11 (RSP11) 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. RSP11 is a non-PKA (cAMP-dependent protein kinase) RIIa protein that contains a RII domain but lack any features required for cAMP signaling or phosphorylation. It is involved in the control of ciliary and flagellar beating. RSP11 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 RSP11 heterodimerizes with the D/D domain of RSP7 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