Conformational switching in the coiled-coil domains of a proteasomal ATPase regulates substrate processing
Proteasomal ATPases contain functionally important coiled-coil (CC) domains, the mechanistic role of which is not fully understood. Here, the authors provide evidence for three distinct CC conformations, showing that CC conformational changes enable ATPases to switch between active and resting state...
Guardado en:
Autores principales: | Aaron Snoberger, Evan J. Brettrager, David M. Smith |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2018
|
Materias: | |
Acceso en línea: | https://doaj.org/article/d753a210f94644cf8f78d72fae386d53 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Coiled-Coil Antagonism Regulates Activity of Venus Flytrap-Domain-Containing Sensor Kinases of the BvgS Family
por: Elodie Lesne, et al.
Publicado: (2018) -
Oligomerization-primed coiled-coil domain interaction with Ubc13 confers processivity to TRAF6 ubiquitin ligase activity
por: Lin Hu, et al.
Publicado: (2017) -
Switching control between three-coil and five-coil modes for six-pole active magnetic bearings
por: Satoshi UENO, et al.
Publicado: (2019) -
Sequence conservation in Plasmodium falciparum alpha-helical coiled coil domains proposed for vaccine development.
por: Caroline Kulangara, et al.
Publicado: (2009) -
Inositol pyrophosphates promote the interaction of SPX domains with the coiled-coil motif of PHR transcription factors to regulate plant phosphate homeostasis
por: Martina K. Ried, et al.
Publicado: (2021)