PSAP(195-273) forms a dimer

Saposin B (PSAP(195-273)) is the only PSAP fragment that forms a dimer. The dimer is disulfide-linked and can switch between two conformations, one of which shows an open hydrophobic pocket, supporting a lipid solubilization mechanism for saposin B, consistent with the observation that saposin B can act as a lipid-transport protein (Vaccaro et al., 1995; Ahn et al., 2002; Ahn et al., 2003).

Saposin B（PSAP(195-273)）是唯一一种能够形成二聚体的PSAP片段。该二聚体通过二硫键连接，能够在两种构象之间切换，其中一种构象呈现出开放的疏水口袋，这一特性支持了saposin B的脂质溶解机制，与saposin B可作为脂质转运蛋白的观察结果相一致（Vaccaro等，1995；Ahn等，2002；Ahn等，2003）。