Mechanism for Dynein Movement
The globular heads of the heavy chain have a ring-structure composed of AAA repeats that project MT-binding stalks. ATP binding alters the AAA repeat domain of one head domain, which frees up its MT binding while ATP hydrolysis allows the head to rebind MTs taking a 8 nm step toward the minus-end. The other head binds ATP and repeats the process leading to processive movement along microtubules. A family of dynein motors distinct from cytoplasmic dynein function in intraflagellar transport in cilia.