Ponting C P
Department of Biochemistry, University of Oxford, United Kingdom.
Protein Sci. 1994 Feb;3(2):359-61. doi: 10.1002/pro.5560030219.
An N-terminal region of the acid sphingomyelinase sequence (residues 89-165) is shown to be homologous to saposin-type sequences. By analogy with the known functions of saposins, this sphingomyelinase saposin-type domain may possess lipid-binding and/or sphingomyelinase-activator properties. This finding may prove to be important in the understanding of Niemann-Pick disease, which results from sphingomyelinase deficiency.
酸性鞘磷脂酶序列的N端区域(第89 - 165位氨基酸残基)显示与鞘脂激活蛋白(saposin)类型的序列具有同源性。通过与鞘脂激活蛋白已知功能进行类比,该鞘磷脂酶的鞘脂激活蛋白类型结构域可能具有脂质结合和/或鞘磷脂酶激活特性。这一发现可能在理解由鞘磷脂酶缺乏引起的尼曼-匹克病方面具有重要意义。