内质网金属肽酶1假定蛋白-蛋白相互作用的计算机模拟分析

In Silico Analysis of Protein-Protein Interactions of Putative Endoplasmic Reticulum Metallopeptidase 1 in .

作者信息

González-Esparragoza Dalia, Carrasco-Carballo Alan, Rosas-Murrieta Nora H, Millán-Pérez Peña Lourdes, Luna Felix, Herrera-Camacho Irma

机构信息

Laboratorio de Bioquímica y Biología Molecular, Centro de Química del Instituto de Ciencias (ICUAP), Benemérita Universidad Autónoma de Puebla, Puebla 72570, Mexico.

Laboratorio de Elucidación y Síntesis en Química Orgánica, Instituto de Ciencias de la Universidad Autónoma de Puebla (ICUAP), Benemérita Universidad Autónoma de Puebla, Puebla 72570, Mexico.

出版信息

Curr Issues Mol Biol. 2024 May 12;46(5):4609-4629. doi: 10.3390/cimb46050280.

DOI:10.3390/cimb46050280

PMID:38785548

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11120530/

Abstract

Ermp1 is a putative metalloprotease from 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 Ca 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是一种来自[具体来源未提及]的假定金属蛋白酶，属于Fxna肽酶家族成员。尽管其功能尚不清楚，但大鼠和人类的直系同源蛋白与卵巢卵泡成熟及内质网应激增加有关。本研究重点通过比较人类和酵母之间的互作同源物，以及Ermp1的M28结构域与可能的靶蛋白的分子对接和动力学，首次提出蛋白质-蛋白质相互作用（PPI）的预测。结果表明，有45种蛋白质可能与该金属蛋白酶相互作用。这些蛋白质大多与钙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结构域可能水解Amk2、Ypt5和Pex12的亮氨酸和蛋氨酸残基。这些结果可为未来对其他Fxna肽酶，如人类ERMP1的实验研究提供支持。