The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity
Plasmodium falciparum moves by an atypical process called gliding motility which comprises of atypical myosin A (PfMyoA) and filaments of the dynamic and divergent PfActin-1 (PfAct1). Here authors present the cryo-EM structure of PfMyoA bound to filamentous PfAct1 stabilized with jasplakinolide and...
Guardado en:
Autores principales: | Julien Robert-Paganin, Xiao-Ping Xu, Mark F. Swift, Daniel Auguin, James P. Robblee, Hailong Lu, Patricia M. Fagnant, Elena B. Krementsova, Kathleen M. Trybus, Anne Houdusse, Niels Volkmann, Dorit Hanein |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/1e9f084757d3479aa82cffe48fcd9158 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Plasmodium myosin A drives parasite invasion by an atypical force generating mechanism
por: Julien Robert-Paganin, et al.
Publicado: (2019) -
Hypertrophic cardiomyopathy disease results from disparate impairments of cardiac myosin function and auto-inhibition
por: Julien Robert-Paganin, et al.
Publicado: (2018) -
Novel interfaces for light directed neuronal stimulation: advances and challenges
por: Bareket-Keren L, et al.
Publicado: (2014) -
Mechanoregulated inhibition of formin facilitates contractile actomyosin ring assembly
por: Dennis Zimmermann, et al.
Publicado: (2017) -
Atomic Identification of Interfaces in Individual Core@shell Quantum Dots
por: Guiju Liu, et al.
Publicado: (2021)