Actin-DBP: the perfect structural fit?

Laboratorium voor Analytische Chemie en Medicinale Fysicochemie, Faculteit Farmaceutische Wetenschappen, K. U. Leuven, Belgium.
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.
Mesh Terms:
Actins, Animals, Binding Sites, Crystallography, X-Ray, Humans, Hydrogen Bonding, Microfilament Proteins, Models, Molecular, Protein Conformation, Protein Structure, Tertiary, Rabbits, Vitamin D-Binding Protein
Acta Crystallogr. D Biol. Crystallogr. Feb. 01, 2003; 59(0);263-73 [PUBMED:12554937]
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