5.6.1.2	all dyneins share a conserved motor domain. The core of the dynein motor domain consists of six tandem AAA+ ATPase domains. The first AAA+ domain (AAA1) is the primary site of ATP hydrolysis, whereas the other five domains (AAA2-6) have regulatory or structural functions. The dynein linker domain acts as a relatively rigid lever that amplifies small conformational changes in the AAA+ domains upon ATP hydrolysis	711714	
5.6.1.2	crystal structure analysis	735286	
5.6.1.2	hanging-drop method, 1.7 A resolution, dynein light chain TcTex-1	669342	
5.6.1.2	hanging-drop vapor diffusion method, dynein light chain Dnlc2A	667449	
5.6.1.2	microtubule-binding domain	701228	
5.6.1.2	resolution of 6 A of a functional dimer of two ca. 300 kDa motor domains of yeast cytoplasmic dynein, which are dimerized by glutathione S-transferase GST. The structure reveals an unusual asymmetric arrangement of ATPase domains and an unexpected interaction between two coiled coils the create a base for the microtubule binding domain	713512	
5.6.1.2	the active sites for microtubule binding and ATP hydrolysis communicate via conformational changes transduced through a ca. 10 nm length antiparallel coilded-coil stalk, which connects the binding domain to the roughly 300 kDa motor core. A balancing of opposing conformations in the stalk and microtubule binding domain (MTBD) enables modest ling-range interactions arising from ATP-binding in the motor core to induce a relaxation of the MTBD into the stable low affinity state	712426