Cargando…
Saturation transfer difference NMR on the integral trimeric membrane transport protein GltPh determines cooperative substrate binding
Saturation-transfer difference (STD) NMR spectroscopy is a fast and versatile method which can be applied for drug-screening purposes, allowing the determination of essential ligand binding affinities (K(D)). Although widely employed to study soluble proteins, its use remains negligible for membrane...
Autores principales: | Hall, Jenny L., Sohail, Azmat, Cabrita, Eurico J., Macdonald, Colin, Stockner, Thomas, Sitte, Harald H., Angulo, Jesus, MacMillan, Fraser |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7536232/ https://www.ncbi.nlm.nih.gov/pubmed/33020522 http://dx.doi.org/10.1038/s41598-020-73443-z |
Ejemplares similares
-
Deciphering structural rearrangements during transport process in the bacterial transporter GltPh, homolog to mammalian glutamate transporter
por: Venkatesan, SanthoshKannan, et al.
Publicado: (2012) -
Refinement of the Central Steps of Substrate Transport by the Aspartate Transporter GltPh: Elucidating the Role of the Na2 Sodium Binding Site
por: Venkatesan, SanthoshKannan, et al.
Publicado: (2015) -
Kinetic mechanism of coupled binding in sodium-aspartate symporter GltPh
por: Oh, SeCheol, et al.
Publicado: (2018) -
The high‐energy transition state of the glutamate transporter homologue GltPh
por: Huysmans, Gerard H M, et al.
Publicado: (2020) -
Structural Intermediates
in a Model of the Substrate
Translocation Path of the Bacterial Glutamate Transporter Homologue
GltPh
por: Stolzenberg, Sebastian, et al.
Publicado: (2012)