Computations based on detailed atomic models explain how the ATP-driven sodium-potassium pump avoids transporting the wrong type of ions in order to maintain the physiological concentration of sodium and potassium ions across the cell membrane.
An auxiliary subunit alters the effect of a family of small-molecule openers on a voltage-gated potassium channel by inducing structural re-arrangements that promote protonation of the drug molecule.
Matthew L Rook, Abby Williamson ... David M Maclean
The rotation of the β11-12 linker is a crucial control point for acid-sensing ion channel gating and motion of this linker is required for the channel to desensitize.
Simon M Lichtinger, Joanne L Parker ... Philip C Biggin
The manner in which protons control the conformational behaviour of mammalian peptide transporters is revealed through state-of-the-art molecular dynamics simulations supported by cell-based assays.
High-performance computing simulations reveal how two remote sites in the multidrug transporter AcrB work together for drug extrusion using the proton-motive force.
Benzene mapping simulations of envelope protein rafts from six different flaviviruses reveal a conserved cryptic site whose cluster of ionisable residues is likely responsible for orchestrating pH-dependent conformational changes during fusion, thereby representing an attractive target for antiviral development.
Poor intracellular availability and diffusion of weakly basic, small molecule drugs can be greatly enhanced by preventing ion trapping in crowded cellular environments.
Masaki Tsujimura, Keiichi Kojima ... Hiroshi Ishikita
Asp234 is deprotonated in the ground state and forms the proton transfer pathway that proceeds from the Schiff base toward Glu68 in the intermediate state of the anion channelrhodopsin GtACR1.
