Article
Crucial role of H322 in folding of the diphtheria toxin T-domain into the open-channel state.
Biochemistry - 21 May 2013
Vargas-Uribe Mauricio, Rodnin Mykola V, Kienker Paul, Finkelstein Alan, Ladokhin Alexey S
Abstract excerpt
The translocation (T) domain plays a key role in the entry of diphtheria toxin into the cell. Upon endosomal acidification, the T-domain undergoes a series of conformational changes that lead to its membrane insertion and formation of a channel. Recently, we have reported that the triple replacement of C-terminal histidines H322, H323, and H372 with glutamines prevents the formation of open channels in planar...
Topics
- Binding Sites
- Circular Dichroism
- Diphtheria Toxin
- Histidine
- Hydrogen-Ion Concentration
- Lipid Bilayers
- Models, Molecular
- Mutation
- Protein Conformation
- Protein Folding
- Tryptophan