Cargando…
Divalent Metal Ion Coordination by Residue T118 of Anthrax Toxin Receptor 2 Is Not Essential for Protective Antigen Binding
The protective antigen (PA) subunit of anthrax toxin interacts with the integrin-like I domains of either of two cellular receptors, ANTXR1 or ANTXR2. These I domains contain a metal ion-dependent adhesion site (MIDAS) made up of five non-consecutive amino acid residues that coordinate a divalent me...
Autores principales: | Scobie, Heather M., Young, John A.T. |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2006
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1762376/ https://www.ncbi.nlm.nih.gov/pubmed/17183731 http://dx.doi.org/10.1371/journal.pone.0000099 |
Ejemplares similares
-
Anthrax Toxin Receptor 2–Dependent Lethal Toxin Killing In Vivo
por: Scobie, Heather M, et al.
Publicado: (2006) -
Correction: Anthrax Toxin Receptor 2–Dependent Lethal Toxin Killing In Vivo
por: Scobie, Heather M, et al.
Publicado: (2008) -
Anthrax Toxin Receptor 2 Determinants that Dictate the pH Threshold of Toxin Pore Formation
por: Scobie, Heather M., et al.
Publicado: (2007) -
Functions of Phenylalanine Residues within the β-Barrel Stem of the Anthrax Toxin Pore
por: Wang, Jie, et al.
Publicado: (2009) -
Engineered allosteric ribozymes that respond to specific divalent metal ions
por: Zivarts, Maris, et al.
Publicado: (2005)