Fig. 5: Species-specific compositions and positions of single-headed IDAs.
From: Axonemal structures reveal mechanoregulatory and disease mechanisms
a, Atomic model of the six single-headed IDAs as they appear on the C. reinhardtii DMT. Each IDA is associated with actin and either centrin or a p28 homodimer; p38 and p44 are specific docking factors for IDAd. b, Cropped image showing the DMT-bound bases of the human single-headed IDAs. Compared with those of C. reinhardtii, IDAb and IDAe have different subunit compositions and docking positions. c,d, Cryo-EM density of the dynein tail domains was used to identify the HC of IDAa as DNAH12 (c) and that of IDAc as DNAH3 (d). e, Cryo-EM map and model showing the molecular environment of IDAg and IDAd and its connection with RS3S in C. reinhardtii. A similar arrangement is found at the base of human RS3. f, The DNALI1 homodimer of human IDAe interacts directly with the tubulin interdimer interface. Similar interactions with tubulin are observed for human IDAa, IDAb and IDAc and their equivalents in C. reinhardtii (through the equivalent p28 homodimer).
