Browse our latest Structural Biology and Molecular Biophysics articles

Evidence is presented that supports a completely new, diffusion-driven mechanism for transporting proteins across membranes in bacteria.

Multimerization plays a functional role in EGFR activation and can be blocked by mutations in a specific region of Domain IV.

Allosteric modulation in the M2 muscarinic receptor derives from a mix of interactions within and between the protomers of an oligomer.

An ensemble of cryo-EM structures reveals how eukaryotic elongation factor 2 positions the first codon of a viral mRNA for translation.

A phage-encoded protein inhibits a bacterial replicative helicase loading factor by exploiting an internal site that auto-regulates loader self-assembly and ATPase activity.

The structure of a multi-protein DNA recombination reaction intermediate reveals how regulation is achieved by protein-mediated DNA wrapping around a core enzyme-substrate complex.

When the Ca²⁺-binding loops of the C2B domain insert into a membrane, interactions with a phospholipid and the SNARE complex allow synaptotagmin-1 to bend the membrane.

Ca_V1.3 channels of the short isoform are coupled via their C-terminal domains in a Ca²⁺-CaM-dependent manner, which facilitates Ca²⁺ influx and increases the discharge of hippocampal neurons.