Browse our latest Structural Biology and Molecular Biophysics articles

The atomic structure of GtACR1 provides new insight into the chemical mechanism of natural light-gated anion membrane conductance, and enables its optimization for optogenetic photoinhibition of neuron firing.

A single kinetic step in the G protein activation cycle determines whether a G protein-coupled receptor activates G protein-gated K⁺ channels or not.

Differences in the kinetics of G protein activation can explain why only some receptors can activate potassium ion channels called GIRKs.

TRPV channels share general mechanisms of activation while exhibiting subtype-specific features along the activation pathway that can determine their apparent sensitivity to stimuli.

The auxiliary protein Stargazin limits the conformational dynamics of AMPA-type glutamate receptors in cell membranes, as revealed by 'molecular rulers' deployed on the seconds to milliseconds timescale.

Sec1/Munc18-family proteins chaperone SNARE assembly via a common templating mechanism.

Synthetic PPARγ ligands push and cobind with natural endogenous ligands, instead of compete and displace, which synergistically affects the structure and function of PPARγ.

Membrane mechanics predict that the ion channel Piezo recruits the surrounding membrane to amplify its sensitivity to changes in membrane tension, with greatest sensitivity in the low-tension regime.

A dual-color TIRFM study reveals a new form of inflammatory regulation, in which a lipid kinase and ion channel reciprocally regulate each other to amplify the response to painful stimuli.

Atomic details on structural organization and conformational dynamics of the key regulator of neuronal signaling shed light on its allosteric regulation and role in regulating cellular pathways.