Dynein structure

Dynein is a complex motor protein consisting of two very large (500 kDa) heavy chains, two intermediate chains and two light chains. Thus like kinesin, dynein is double headed having two microtubule binding domains. The Dynein heavy chain contains an N-terminus tail which binds the Dynactin complex (to bind cargo) and a C-terminus composed of 6 AAA ATPase domains which are arranged in a wheel. The C- terminal ATPase domain closes the wheel by forming contacts with the first AAA domain which is the major ATPase that generates the conformational change which alters the position of the tail relative to the ATPase wheel. A stalk region in between AAA domains 4 and 5 binds the microtubule.