Dynein heavy chain, ATP-binding dynein motor region
IPR035706
Definition
This is the fifth AAA+ domain subdomain AAA5S. Structural analysis reveal that it is the coiled-coil buttress interface. The relative movement of AAA5S together with the stalk (AAA4S), is coupled to rearrangements in the AAA+ ring. Closure of the AAA1 site and the rigid body movement of AAA2-AAA4 force the AAA4/AAA5 interface to close and the AAA6L subdomain to rotate towards the ring centre. The AAA5S subdomain rotates as a unit together with AAA6L, and this movement pulls the buttress relative to the stalk PMID:25470043. Dyneins are motor proteins of eukaryotic cells that convert energy from ATP hydrolysis into force and movement along microtubules. They generally contain one to three heavy chains (each >500kDa), which belong to the AAA+ superfamily of mechanochemical enzymes, along with several accessory subunits ranging from light to intermediate chains. Each heavy chain consists of a flexible N-terminal tail known as the cargo-binding domain and a motor domain. The motor domain comprises an ATP-hydrolysing AAA+ ring (formed by six AAA domains), a linker, a stem, a C-sequence, and a stalk with a long coiled-coil structure. The stalk contains an ATP-sensitive microtubule-binding site at its tip, while the linker functions as a mechanical element for generating dynein's power stroke. Studies using a 380kDa recombinant fragment of the Dictyostelium dynein heavy chain demonstrated that the C-terminal two-thirds maintains microtubule-activated ATPase activity and drives robust microtubule sliding, confirming this region as the functional motor domain PMID:22398446. Two categories of dyneins exist: axonemal dyneins, which produce bending motions that propagate along cilia and flagella, and cytoplasmic dyneins, which drive fundamental cellular processes including nuclear migration, mitotic spindle organisation, chromosome separation, and the positioning and function of intracellular organelles [[cite:PMID:16061793], [cite:PMID:8666668], [cite:PMID:16229832]].
14 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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