PDF(Pubmed)
Abstract：
Ermp1 is a putative metalloprotease from Schizosaccharomyces pombe and a member of the Fxna peptidases. Although their function is unknown, orthologous proteins from rats and humans have been associated with the maturation of ovarian follicles and increased ER stress. This study focuses on proposing the first prediction of PPI by comparison of the interologues between humans and yeasts, as well as the molecular docking and dynamics of the M28 domain of Ermp1 with possible target proteins. As results, 45 proteins are proposed that could interact with the metalloprotease. Most of these proteins are related to the transport of Ca2+ and the metabolism of amino acids and proteins. Docking and molecular dynamics suggest that the M28 domain of Ermp1 could hydrolyze leucine and methionine residues of Amk2, Ypt5 and Pex12. These results could support future experimental investigations of other Fxna peptidases, such as human ERMP1.
摘要：
Ermp1是来自裂殖酵母的推定金属蛋白酶，也是Fxna肽酶的成员。虽然它们的功能是未知的，来自大鼠和人类的直系同源蛋白与卵巢卵泡成熟和内质网应激增加有关.这项研究的重点是通过比较人类和酵母之间的相互作用，提出PPI的第一个预测，以及Ermp1的M28结构域与可能的靶蛋白的分子对接和动力学。作为结果，提出了45种可以与金属蛋白酶相互作用的蛋白质。这些蛋白质中的大多数与Ca2的运输以及氨基酸和蛋白质的代谢有关。对接和分子动力学表明，Ermp1的M28结构域可以水解Amk2，Ypt5和Pex12的亮氨酸和蛋氨酸残基。这些结果可以支持其他Fxna肽酶的未来实验研究，例如人类ERMP1。
