Browse our latest Structural Biology and Molecular Biophysics articles

The voltage-sensing mechanism of a subfamily of potassium channels is modulated in unconventional ways by an amino acid transporter.

Cryo-EM shows that the NADase activity of SARM1 is allosterically inhibited by physiological concentrations of NAD+ that stabilizes an auto-inhibited conformation of SARM1, explaining how NAD+ depletion may inflict neurodegeneration.

Poxin enzymes are a diverse family of insect and viral 2′3′-cGAMP nucleases, which evolved from self-cleaving RNA virus accessory proteases.

Substrate releasing or inhibitor binding on the intracellular side of a glutamate transporter homologue require movements of the transport domain through the lipid membrane, which undergoes adaptive deformations.

Electrophysiological and molecular modeling studies identify a sulfur-aromatic interaction between the hydrophobic channel gate and a nearby methionine residue, termed the "gate latch", which is essential for Orai1 pore opening.

Novel capsaicin analogs with conserved chemistry but varying sizes were used as molecular rulers to investigate energetics of conformational changes in the ligand-binding pocket and mechanisms of TRPV1 ligand-gating.

A generalizable approach to understanding the logic of molecular recognition reveals the contributions of individual residues to the specificity of protein-protein interactions.

Cryo-electron microscopic structures of 5-HT₃A receptor in complex with first and second generations of clinically used setron reveal the molecular basis for their binding modes and mechanisms of inhibitory action.

Cryo-EM structures of the AAA+ ClpXP protease bound to an ssrA degron reveal the mechanism of substrate recognition and show how the machine transitions from recognition to translocation and unfolding.

Structures of CdiB outer membrane transporters reveal the channel-gating mechanism for the secretion of large bacterial toxins.