Hepsin is the first protease identified to modulate specific cleavage and secretion of a Zona Pellucida domain protein, uromodulin.

Comparative structural studies reveal how the cytoplasmic tails of Eph receptors can differentiate different downstream target proteins via highly specific SAM–SAM domain interactions.

Structure/function studies of a plant pathogen effector in complex with a host disease resistance protein domain reveal the molecular basis for recognition and underpin future engineering of immunity in crops.

A cysteine-rich domain within the Smoothened receptor may represent a novel therapeutic target for cancers caused by abnormal functioning of the Hedgehog signaling pathway.

The C2-domain of cytoplasmic phospholipase A₂α is structurally designed to target PC-rich membrane regions to increase the enzymatic efficiency of the catalytic domain, which prefers PCs with polyunsaturated acyl chains.

Analysis of the E. coli protein DolP reveals the first dual BON-domain structure and identifies phospholipid binding as a new mechanism for protein localisation to the outer membrane division site.

Unbiased molecular dynamics simulations reveal the insertion mechanism of the lipidated tail of the matrix domain of HIV-1 Gag into realistic membrane models and show its effect on lipid sorting.

A new structure reveals two Arf-GEF regulatory domains form a single structural unit that stimulates Arf-GEF activity.

Rab6A binds directly to both the C-terminus and the N-terminal motor domain of the kinesin KIF1C to regulate vesicle motility and Golgi organization.

Overcoming image-processing problems in the analysis of the ClpB chaperone provides a new structural model and regulatory mechanism, based on clear density for the coiled-coil domain and supported by various biochemical data.