New Aspects of DBP

The Vitamin D Binding Protein DBP

“…Although the folding within each corresponding domain shows some parallels, the global orientation of the three domains in both molecules is strikingly different, resulting in two totally different structures. Residual electron density that can accommodate 25(OH)D 3 is observed in DBP holoprotein, close to the biochemically identified vitamin-D-binding residues [10,11]. Residues belonging to helices 1e6 of domain I form the complete vitamin-Dbinding site (Fig.…”

“…In low-salt buffers actin exists as a monomeric protein (globular actin, G-actin), but it polymerizes under physiological salt conditions into a double helical 10-nm-thick filament structure (filamentous actin, Factin). In vivo, the equilibrium between G-actin and Factin is controlled mainly by the action of several actin-binding proteins with distinct activities (e.g., gelsolin or profilin) [11].…”