Vasohibins play a crucial role in regulating processes like angiogenesis, tumor growth, and neuronal differentiation through their interaction with the small vasohibin-binding protein (SVBP).
Recent studies, including crystal structure determinations, have revealed insights into the complex's formation and function, but the regulatory mechanisms remain unclear.
This research specifically highlights the discovery of a novel domain-swapped heterotetramer structure that may influence enzyme activity due to the stabilization provided by conserved residues and differences in molecular dynamics compared to simpler structures.