In the extremely selective fluoride channels from the bacterial Fluc family, fluoride ions access the pore via two points, an electropositive vestibule and a triad of conserved residues involved in anion recognition.
Combining crystal structures with single-pore analysis of Fluc-family fluoride channel mutants demonstrates that Fluc channels have two separate fluoride ion permeation pathways within the channel complex.
The structure-based design established a new approach to control pathway-selective activation of opioid receptors, resulting in new dual MOR/KOR G-protein biased agonist analgesics with attenuated liabilities.
In behaving mice, inhibition from molecular layer interneurons attenuates excitation of Purkinje cells by parallel fibers and suppresses their ability to enhance climbing fiber-triggered dendritic Ca2+ responses.
Standing genetic variation for disease resistance may be continuously lost during recurring warm water episodes because of widespread susceptibility of disease-resistant genotypes to bleaching and the independence between these two traits.