Figure 1. Human dynein-1 and dynein-2. A, B: Schematic representation of human dynein heavy chain DYNC1H1 (A) and DYNC2H1 (B) domain structures. DD, dimerization domain; NTD, N-terminal domain; DIC, dynein intermediate chain interaction site; LI, light intermediate interaction site; blue bars, ATPase domains 1–6; stalk; MBD, microtubule-binding domain; CTD, C-terminal domain. Numbers at the C-terminus indicate amino acids in the human and mouse, with those of the mouse enclosed by parentheses. Adapted from [88] and [59]. The 500 aa bar indicates the length occupied by 500 amino acids. C, D: representations of multimeric dynein-1 and dynein-2. The heavy chains form homodimers, the scaffolds of which organize the distributions of intermediate, light intermediate, and light chains (adapted from [45] and [33]. The N-terminal 200 amino acids represent the dimerization domain (dim).