Cargando…
pH-Triggered Conformational Switching along the Membrane Insertion Pathway of the Diphtheria Toxin T-Domain
The translocation (T)-domain plays a key role in the action of diphtheria toxin and is responsible for transferring the catalytic domain across the endosomal membrane into the cytosol in response to acidification. Deciphering the molecular mechanism of pH-dependent refolding and membrane insertion o...
Autor principal: | Ladokhin, Alexey S. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3760040/ https://www.ncbi.nlm.nih.gov/pubmed/23925141 http://dx.doi.org/10.3390/toxins5081362 |
Ejemplares similares
-
Structure of the Diphtheria Toxin at Acidic pH: Implications for the Conformational Switching of the Translocation Domain
por: Rodnin, Mykola V., et al.
Publicado: (2020) -
Hydrogen–Deuterium Exchange and Mass Spectrometry Reveal the pH-Dependent
Conformational Changes of Diphtheria Toxin T Domain
por: Li, Jing, et al.
Publicado: (2014) -
Histidine Protonation and Conformational Switching in Diphtheria Toxin Translocation Domain
por: Rodnin, Mykola V., et al.
Publicado: (2023) -
Role of Acidic Residues in Helices TH8–TH9 in Membrane Interactions of the Diphtheria Toxin T Domain
por: Ghatak, Chiranjib, et al.
Publicado: (2015) -
Cellular Entry of the Diphtheria Toxin Does Not Require the Formation of the Open-Channel State by Its Translocation Domain
por: Ladokhin, Alexey S., et al.
Publicado: (2017)