The amoebapore superfamily

Yufeng Zhai, Milton H Saier Jr.
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引用次数: 63

Abstract

Amoebapores, synthesized by human protozoan parasites, form ion channels in target cells and artificial lipid membranes. The major pathogenic effect of these proteins is due to their cytolytic capability which results in target cell death. They comprise a coherent family and are homologous to other proteins and protein domains found in eight families. These families include in addition to the amoebapores (1) the saposins, (2) the NK-lysins and granulysins, (3) the pulmonary surfactant proteins B, (4) the acid sphingomyelinases, (5) acyloxyacyl hydrolases and (6) the aspartic proteases. These amoebapore homologues have many properties in common including membrane binding and stability. We note for the first time that a new protein, countin, from the cellular slime mold, Dictyostelium discoideum, comprises the eighth family within this superfamily. All currently sequenced members of these eight families are identified, and the structural, functional and phylogenetic properties of these proteins are discussed.

阿米巴虫超家族
变形虫是由人类原生动物寄生虫合成的,在靶细胞和人工脂膜中形成离子通道。这些蛋白的主要致病作用是由于它们的细胞溶解能力,导致靶细胞死亡。它们组成了一个连贯的家族,与八个家族中发现的其他蛋白质和蛋白质结构域同源。除了变形虫外,这些家族还包括(1)皂苷,(2)nk -溶酶和颗粒溶酶,(3)肺表面活性剂蛋白B,(4)酸性鞘磷脂酶,(5)酰基酰水解酶和(6)天冬氨酸蛋白酶。这些阿米巴虫同源物有许多共同的性质,包括膜结合和稳定性。我们第一次注意到,一个新的蛋白质,计数,从细胞黏菌,盘状盘霉,包括第八家族在这个超家族。鉴定了这8个家族的所有已测序成员,并讨论了这些蛋白质的结构、功能和系统发育特性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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