Cargando…
QacR−Cation Recognition Is Mediated by a Redundancy of Residues Capable of Charge Neutralization†
[Image: see text] The Staphylococcus aureus multidrug binding protein QacR binds to a broad spectrum of structurally dissimilar cationic, lipophilic drugs. Our previous structural analyses suggested that five QacR glutamic acid residues are critical for charge neutralization and specification of cer...
Autores principales: | Peters, Kate M., Schuman, Jason T., Skurray, Ronald A., Brown, Melissa H., Brennan, Richard G., Schumacher, Maria A. |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2008
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2646753/ https://www.ncbi.nlm.nih.gov/pubmed/18616285 http://dx.doi.org/10.1021/bi8008246 |
Ejemplares similares
-
A Single Acidic Residue Can Guide Binding Site Selection but Does Not Govern QacR Cationic-Drug Affinity
por: Peters, Kate M., et al.
Publicado: (2011) -
Functional analyses reveal an important role for tyrosine residues in the staphylococcal multidrug efflux protein QacA
por: Wu, Jingqin, et al.
Publicado: (2008) -
Efflux Pump (QacA, QacB, and QacC) and β-Lactamase Inhibitors? An Evaluation of 1,8-Naphthyridines against Staphylococcus aureus Strains
por: Oliveira-Tintino, Cícera Datiane de Morais, et al.
Publicado: (2023) -
The role of TMS 12 in the staphylococcal multidrug efflux protein QacA
por: Dashtbani-Roozbehani, Abolfazl, et al.
Publicado: (2023) -
Anion Recognition by Neutral and Cationic Iodotriazole Halogen Bonding Scaffolds
por: Iribarren, Iñigo, et al.
Publicado: (2020)