A nanobody suite for yeast scaffold nucleoporins provides details of the nuclear pore complex structure
Characterizing the assembly of the nuclear pore complex (NPC) remains challenging. Here, the authors develop a set of nanobodies that recognize seven constituent nucleoporins, study their binding characteristics, and apply them to probe accessible and obstructed NPC surfaces in yeast.
Guardado en:
Autores principales: | Sarah A. Nordeen, Kasper R. Andersen, Kevin E. Knockenhauer, Jessica R. Ingram, Hidde L. Ploegh, Thomas U. Schwartz |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2020
|
Materias: | |
Acceso en línea: | https://doaj.org/article/08cecb6773264203972c596074acd9d4 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Nucleoporin 153 links nuclear pore complex to chromatin architecture by mediating CTCF and cohesin binding
por: Shinichi Kadota, et al.
Publicado: (2020) -
Yeast Nup84-Nup133 complex structure details flexibility and reveals conservation of the membrane anchoring ALPS motif
por: Sarah A. Nordeen, et al.
Publicado: (2020) -
Higher nucleoporin-Importinβ affinity at the nuclear basket increases nucleocytoplasmic import.
por: Mohammad Azimi, et al.
Publicado: (2013) -
Improved GPCR ligands from nanobody tethering
por: Ross W. Cheloha, et al.
Publicado: (2020) -
DNA origami scaffold for studying intrinsically disordered proteins of the nuclear pore complex
por: Philip Ketterer, et al.
Publicado: (2018)