Structural, computational and functional approaches reveal the role of an extended acidic chamber near the nucleotide binding site in activation of P2X3 receptor channels by divalent-bound ATP.
Multi-site FRET measurements of moPrP oligomerization at low pH indicate that major conformational changes take place as monomers reversibly transform into large oligomers, which subsequently disassemble reversibly into small oligomers.
Single molecule subunit counting, FRET and electrophysiology experiments reveal that metabotropic glutamate receptor subunits interact and rearrange at the level of the transmembrane domains in response to allosteric modulators.
The vesicular Ca2+ sensor synaptotagmin-1 regulates both fast phasic and slow tonic glutamate release at ribbon synapses of rod and cone photoreceptor cells.
