Cargando…
The Conserved Lysine-265 Allosterically Modulates Nucleotide- and Actin-binding Site Coupling in Myosin-2
Myosin motor proteins convert chemical energy into force and movement through their interactions with nucleotide and filamentous actin (F-actin). The evolutionarily conserved lysine-265 (K265) of the myosin-2 motor from Dictyostelium discoideum (Dd) is proposed to be a key residue in an allosteric c...
Autores principales: | Behrens, Vincent A., Münnich, Stefan, Adler-Gunzelmann, Georg, Thiel, Claudia, Henn, Arnon, Latham, Sharissa L., Taft, Manuel H. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5550493/ https://www.ncbi.nlm.nih.gov/pubmed/28794442 http://dx.doi.org/10.1038/s41598-017-07933-y |
Ejemplares similares
-
Three mammalian tropomyosin isoforms have different regulatory effects on nonmuscle myosin-2B and filamentous β-actin in vitro
por: Pathan-Chhatbar, Salma, et al.
Publicado: (2018) -
Distinct actin–tropomyosin cofilament populations drive the functional diversification of cytoskeletal myosin motor complexes
por: Reindl, Theresia, et al.
Publicado: (2022) -
Allosteric regulation by cooperative conformational changes of actin filaments drives mutually exclusive binding with cofilin and myosin
por: Ngo, Kien Xuan, et al.
Publicado: (2016) -
Distinct Functional Interactions between Actin Isoforms and Nonsarcomeric Myosins
por: Müller, Mirco, et al.
Publicado: (2013) -
Not actin, not myosin, but intermediate
por: Bonetta, Laura
Publicado: (2005)