Cytoplasmic dynein is a large protein complex that has two heavy chains along with several lighter chains. The N-terminal region (or the tail) of the heavy chain behaves as an assembly platform for the accessory chains, while the the motor domain (located at the C-Terminal) hydrolyses the ATP and is responsible for powering the movement along the microtubule.[1] The heavy chains have a molecular weight of about 0.5-0.6 MDa each, depending on the species. The dynein heavy chain contains a ring structure having six AAA+ subunits. AAA1-AAA4 have the ability to bind ATP while AAA5 and AAA6 do not. The AAA1 has been identified as the major hydrolysis site.[2]
References edit
- ^ Schmidt, Helgo; Carter, Andrew P. (2016-08-01). "Review: Structure and mechanism of the dynein motor ATPase". Biopolymers. 105 (8): 557–567. doi:10.1002/bip.22856. ISSN 1097-0282. PMC 4879348. PMID 27062277.
{{cite journal}}: CS1 maint: PMC format (link) - ^ Höök, Peter. "The Mechanical Components of the Dynein Motor". The Scientific World Journal. 10: 857–864. doi:10.1100/tsw.2010.76.
{{cite journal}}: CS1 maint: unflagged free DOI (link)