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The crystal structure of the actin-DBP complex at 2.4 A resolution reveals an unusually large actin-binding interface, establishing DBP as a highly effective actin-sequestering protein.
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Highlights DBP as potent actin sequesterer; leaves open clinical translation pending functional validation.
The multifunctional vitamin D binding protein (DBP) is an actin-sequestering protein present in blood. The crystal structure of the actin-DBP complex was determined at 2.4 A resolution. DBP binds to actin subdomains 1 and 3 and occludes the cleft at the interface between these subdomains. Most remarkably, DBP demonstrates an unusually large actin-binding interface, far exceeding the binding-interface areas reported for other actin-binding proteins such as profilin, DNase I and gelsolin. The fast-growing side of actin monomers is blocked completely through a perfect structural fit with DBP, demonstrating how DBP effectively interferes with actin-filament formation. It establishes DBP as the hitherto best actin-sequestering protein and highlights its key role in suppressing and preventing extracellular actin polymerization.
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Verboven et al. (2003) studied this question. Vitamin D binding protein (DBP) was evaluated on Crystal structure of the actin-DBP complex. The crystal structure of the actin-DBP complex at 2.4 A resolution reveals an unusually large actin-binding interface, establishing DBP as a highly effective actin-sequestering protein.
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