title: Solution structure of a dynein motor domain associated light chain.
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.
authors.affiliation: Department of Biochemistry, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, Connecticut 06032-3305, USA.
authors.forename: H
authors.initials: H
authors.lastname: Wu
authors.forename: M W
authors.initials: MW
authors.lastname: Maciejewski
authors.forename: A
authors.initials: A
authors.lastname: Marintchev
authors.forename: S E
authors.initials: SE
authors.lastname: Benashski
authors.forename: G P
authors.initials: GP
authors.lastname: Mullen
authors.forename: S M
authors.initials: SM
authors.lastname: King
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D016825:Chlamydomonas reinhardtii / Q000737:chemistry* / Q000166:cytology; D004398:Dyneins / Q000737:chemistry* / Q000378:metabolism*; D005407:Flagella / Q000737:chemistry; D006801:Humans; D008869:Microtubule-Associated Proteins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017413:Ribonucleoprotein, U2 Small Nuclear / Q000737:chemistry; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D012996:Solutions; D013329:Structure-Activity Relationship; D013499:Surface Properties
chemical_list: D004398:Dyneins; D008869:Microtubule-Associated Proteins; D020409:Molecular Motor Proteins; D017413:Ribonucleoprotein, U2 Small Nuclear; D012996:Solutions; C484318:SNRPA1 protein, human