Ontology highlight
ABSTRACT:
SUBMITTER: Marius P
PROVIDER: S-EPMC3236287 | biostudies-literature | 2012 Jan
REPOSITORIES: biostudies-literature
Biochimica et biophysica acta 20110922 1
The activity of the potassium channel KcsA is tightly regulated through the interactions of anionic lipids with high-affinity non-annular lipid binding sites located at the interface between the channel's subunits. Here we present solid-state phosphorous NMR studies that resolve the negatively charged lipid phosphatidylglycerol within the non-annular lipid-binding site. Perturbations in chemical shift observed upon the binding of phosphatidylglycerol are indicative of the interaction of positive ...[more]