LC1 is a 22-kDa leucine-rich repeat (LRR) protein that is bound to the ATP hydrolytic site within the g heavy chain motor domain of Chlamydomonas outer arm dynein. An R196G mutant of LC1 causes cell to swim slowly and undergo frequent reorientation, suggesting that LC1 provides regulatory control of dynein motor function. Backbone dynamics analysis revealed that the C-terminal helix (which contains R196) may undergo significant motion due to the high flexibility of two residues within the connecting loop. Furthermore, the central barrel domain of LC1 contains a flexible hydrophobic spine that provides a heavy chain binding interface. The residues involved form part of the LRR consensus and their high mobility is likely a general feature of this protein class.
Wu, H., Maciejewski, M.W., Marintchev, A., Benashski, S.E., Mullen, G.P. and King, S. M.(2000) Solution structure of a dynein motor domain-associated light chain. Nature Structural Biology, 7, 575-579.