Download MendeleySolution structure of a dynein motor domain associated light chain.
Wu, H., Maciejewski, M.W., Marintchev, A., Benashski, S.E., Mullen, G.P., King, S.M.(2000) Nat Struct Biol 7: 575-579
- PubMed: 10876244
- DOI: https://doi.org/10.1038/76804
- Primary Citation of Related Structures:
1DS9 - PubMed Abstract:
Dyneins are molecular motors that translocate towards the minus ends of microtubules. In Chlamydomonas flagellar outer arm dynein, light chain 1 (LC1) associates with the nucleotide binding region within the gamma heavy chain motor domain and consists of a central leucine-rich repeat section that folds as a cylindrical right handed spiral formed from six beta-beta-alpha 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.
Organizational Affiliation:
Department of Biochemistry, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, Connecticut 06032-3305, USA.
