Structural highlights
Function
DNAL1_CHLRE Associates with the gamma heavy chain in the outer arm dynein. May target p45 polypeptide (an 45 kDa axonemal component) to the motor domain of the gamma heavy chain dynein.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Solution structure of a dynein motor domain associated light chain.,Wu H, Maciejewski MW, Marintchev A, Benashski SE, Mullen GP, King SM Nat Struct Biol. 2000 Jul;7(7):575-9. PMID:10876244[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Benashski SE, Patel-King RS, King SM. Light chain 1 from the Chlamydomonas outer dynein arm is a leucine-rich repeat protein associated with the motor domain of the gamma heavy chain. Biochemistry. 1999 Jun 1;38(22):7253-64. PMID:10353837 doi:http://dx.doi.org/10.1021/bi990466y
- ↑ Wu H, Maciejewski MW, Marintchev A, Benashski SE, Mullen GP, King SM. Solution structure of a dynein motor domain associated light chain. Nat Struct Biol. 2000 Jul;7(7):575-9. PMID:10876244 doi:10.1038/76804
