Chantalat L, Skoufias D A, Kleman J P, Jung B, Dideberg O, Margolis R L
Laboratoire de Cristallographie Macromoléculaire, Institut de Biologie Structurale Jean-Pierre Ebel, CEA-CNRS, Grenoble, France.
Mol Cell. 2000 Jul;6(1):183-9.
Survivin is a mitotic spindle-associated protein involved in linking mitotic spindle function to activation of apoptosis in mammalian cells. The structure of the full-length human survivin has been determined by X-ray crystallography to 2.7 A. Strikingly, the structure forms a very unusual bow tie-shaped dimer. It does not dimerize through a C-terminal coiled-coil, contrary to sequence analysis prediction. The C-terminal helices contain hydrophobic clusters with the potential for protein-protein interactions. The unusual shape and dimensions of survivin suggest it serves an adaptor function through its alpha-helical extensions.
生存素是一种与有丝分裂纺锤体相关的蛋白质，参与将有丝分裂纺锤体功能与哺乳动物细胞凋亡激活联系起来。全长人源生存素的结构已通过X射线晶体学确定为2.7埃。引人注目的是，该结构形成了一种非常不寻常的领结形二聚体。与序列分析预测相反，它不是通过C端卷曲螺旋形成二聚体。C端螺旋包含具有蛋白质-蛋白质相互作用潜力的疏水簇。生存素不寻常的形状和尺寸表明它通过其α螺旋延伸发挥衔接子功能。
