Verboven Christel, Bogaerts Ilse, Waelkens Etienne, Rabijns Anja, Van Baelen Hugo, Bouillon Roger, De Ranter Camiel
Laboratorium voor Analytische Chemie en Medicinale Fysicochemie, Faculteit Farmaceutische Wetenschappen, K. U. Leuven, Belgium.
Acta Crystallogr D Biol Crystallogr. 2003 Feb;59(Pt 2):263-73. doi: 10.1107/s0907444902021455. Epub 2003 Jan 23.
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.
多功能维生素D结合蛋白（DBP）是一种存在于血液中的肌动蛋白隔离蛋白。肌动蛋白-DBP复合物的晶体结构以2.4埃的分辨率确定。DBP与肌动蛋白亚结构域1和3结合，并封闭这些亚结构域之间界面处的裂隙。最显著的是，DBP表现出异常大的肌动蛋白结合界面，远远超过了其他肌动蛋白结合蛋白（如原肌球蛋白、脱氧核糖核酸酶I和凝溶胶蛋白）报道的结合界面面积。肌动蛋白单体快速生长的一侧通过与DBP的完美结构契合而被完全阻断，这表明DBP如何有效地干扰肌动蛋白丝的形成。这确立了DBP作为迄今为止最佳的肌动蛋白隔离蛋白，并突出了其在抑制和防止细胞外肌动蛋白聚合中的关键作用。
Zotero 插件