Cryo-EM structure of 5-HT3A receptor in its resting conformation
Serotonin receptor (5-HT3AR), a pentameric ligand-gated ion channel, regulates numerous gastrointestinal functions. Here the authors provide a cryo-electron microscopic structure from the full-length 5-HT3AR in the apo-state which corresponds to a resting conformation of the channel.
Guardado en:
Autores principales: | Sandip Basak, Yvonne Gicheru, Amrita Samanta, Sudheer Kumar Molugu, Wei Huang, Maria la de Fuente, Taylor Hughes, Derek J. Taylor, Marvin T. Nieman, Vera Moiseenkova-Bell, Sudha Chakrapani |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2018
|
Materias: | |
Acceso en línea: | https://doaj.org/article/1bb90dff34df4dafbd0d19b7edd091cb |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Molecular mechanism of setron-mediated inhibition of full-length 5-HT3A receptor
por: Sandip Basak, et al.
Publicado: (2019) -
Structure of the full-length TRPV2 channel by cryo-EM
por: Kevin W. Huynh, et al.
Publicado: (2016) -
Mechanisms of activation and desensitization of full-length glycine receptor in lipid nanodiscs
por: Arvind Kumar, et al.
Publicado: (2020) -
Structural insights on TRPV5 gating by endogenous modulators
por: Taylor E. T. Hughes, et al.
Publicado: (2018) -
Pathological conformations of disease mutant Ryanodine Receptors revealed by cryo-EM
por: Kellie A. Woll, et al.
Publicado: (2021)