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首页> 外文期刊>Journal of Molecular Biology >Peptide binding by catalytic domains of the protein disulfide isomerase-related protein ERp46
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Peptide binding by catalytic domains of the protein disulfide isomerase-related protein ERp46

机译：蛋白质与二硫键异构酶相关蛋白ERp46的催化域结合的肽

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摘要

The protein disulfide isomerase (PDI) family member ERp46/endoPDI/ thioredoxin domain-containing protein 5 is preferentially expressed in a limited number of tissues, where it may function as a survival factor for nitrosative stress in vivo. It is involved in insulin production as well as in adiponectin signaling and interacts specifically with the redox-regulatory endoplasmic reticulum proteins endoplasmic oxidoreductin 1α (Ero1α) and peroxiredoxin-4. Here, we show that ERp46, although lacking a PDI-like redox-inactive b′-thioredoxin domain with its hydrophobic substrate binding site, is able to bind to a large pool of peptides containing aromatic and basic residues via all three of its catalytic domains (a0, a and a′), though the a0 domain may contain the primary binding site. ERp46, which shows relatively higher activity as a disulfide-reductase than as an oxidase/isomerase in vitro compared to PDI and ERp57, possesses chaperone activity in vivo, a property also shared by the C-terminal a′ domain. A crystal structure of the a′ domain is also presented, offering a view of possible substrate binding sites within catalytic domains of PDI proteins.
机译：蛋白质二硫键异构酶（PDI）家族成员ERp46 / endoPDI /含硫氧还蛋白结构域的蛋白质5在有限数量的组织中优先表达，在其中它可能是体内亚硝化应激的生存因子。它参与胰岛素的产生以及脂联素的信号传导，并且与氧化还原调节的内质网蛋白内质氧化还原蛋白1α（Ero1α）和过氧化物酶4特异性相互作用。在这里，我们表明，ERp46尽管缺乏具有疏水底物结合位点的PDI样氧化还原无活性b'-硫氧还蛋白结构域，但能够通过其所有三个催化结构域与包含芳香族和碱性残基的大量肽结合（a0，a和a'），尽管a0域可能包含主要结合位点。与PDI和ERp57相比，ERp46在体外具有比二氧化还原酶更高的活性，而在体外具有比氧化酶/异构酶更高的活性，它在体内具有分子伴侣活性，C末端a'结构域也具有这种特性。还显示了a'域的晶体结构，提供了PDI蛋白质催化域内可能的底物结合位点的视图。

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