Dyneins are molecular motors that translocate towards the minus ends of microtubules. In Chlamydomon as flagellar outer arm dynein, light chain 1 (LC1) associates with the nucleotide binding region within the γ heavy chain motor domain and consists of a central leucine-rich repeat section that folds as a cylindrical right handed spiral formed from six β-β-α motifs. This central cylinder is flanked by terminal helical subdomains. The C-terminal helical domain juts out from the cylinder and is adjacent to a hydrophobic surface within the repeat region that is proposed to interact with the dynein heavy chain. The position of the C-terminal domain on LC1 and the unexpected structural similarity between LC1 and U2A′ from the human spliceosome suggest that this domain interacts with the dynein motor domain.
Stephen M King合作论文数6Gp Mullen合作论文数5Hongwei Wu合作论文数5Mark W. Maciejewski合作论文数Department of Biochemistry;University of Connecticut;Health Center;Health Center, University of Connecticut5DiBella Linda M合作论文数1Ramila Patel-King合作论文数Department of Molecular Biology and Biophysics, University of Connecticut Health Center1Hugo W. Tedford合作论文数1
Assen Marintchev合作论文数1
Alistair Harrison合作论文数The Center for Microbial Pathogenesis in Nationwide Children's Research Institute and The Center for Microbial Interface Biology, The Ohio State University1
