脂质双层中镁与CX26连接子的相互作用。,Journal of Molecular Modeling

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脂质双层中镁与CX26连接子的相互作用。
Journal of Molecular Modeling ( IF 2.1 ) Pub Date : 2019-07-20 , DOI: 10.1007/s00894-019-4121-5
Juan M R Albano _{1,

2} , Julio C Facelli ₃ , Marta B Ferraro _{1,

2} , Monica Pickholz _{1,

2}

Affiliation

在我们之前的工作中，我们描述了钙与Cx26半通道的相互作用之后，我们通过考虑不同的二阳离子镁的原子分子动力学模拟进一步探索了相同的系统。具体而言，研究了镁阳离子与先前报道的钙结合位点（ASP2，ASP117，ASP159，GLU114，GLU119，GLU120和VAL226）之间的相互作用，以确定它们之间的相似性和差异。为此，进行了四次广泛的模拟。他们中的两个人认为Cx26半通道嵌在具有双阳离子和钠氯溶液之一的POPC双层上。对于其余两个，不包括任何阳离子，并考虑使用钠-氯或钾-氯溶液。钾的原子量类似于钙，钠的原子量类似于镁，但是它们的收费不同（分别为1e和2e）。镁和钙即使具有相同的电荷，对所探查蛋白质的亲和力也不同。从上面提到的钙结合位点，我们发现镁二阳离子仅强烈结合一种连接蛋白的GLU114位点。对于钠和钾的模拟，未发现与蛋白质的特异性相互作用。总而言之，这些结果表明质量效应和空间效应在决定阳离子与Cx26半通道的结合中起着重要作用。对于钠和钾的模拟，未发现与蛋白质的特异性相互作用。总而言之，这些结果表明质量效应和空间效应在决定阳离子与Cx26半通道的结合中起着重要作用。对于钠和钾的模拟，未发现与蛋白质的特异性相互作用。总而言之，这些结果表明质量效应和空间效应在决定阳离子与Cx26半通道的结合中起着重要作用。

"点击查看英文标题和摘要"

Magnesium interactions with a CX26 connexon in lipid bilayers.

Following our previous work, where we described the interaction of calcium with the Cx26 hemichannel, we further explore the same system by atomistic molecular dynamics simulations considering a different di-cation, magnesium. Specifically, the interaction of magnesium di-cation with the previously reported calcium binding sites (ASP2, ASP117, ASP159, GLU114, GLU119, GLU120, and VAL226) was investigated to identify similarities and differences between them. In order to do so, four extensive simulations were carried out. Two of them considered a Cx26 hemichannel embedded on a POPC bilayer with one of the di-cations and a sodium-chlorine solution. For the remaining two, no di-cations were included and a sodium-chlorine or potassium-chlorine solution was considered. Potassium has a similar atomic mass to calcium, and sodium to magnesium, but they both differ in charge (1e and 2e respectively). Magnesium and calcium, even having the same charge, showed different affinity for the explored protein. From the calcium binding sites referred above, we found that the magnesium di-cations only binds strongly to the GLU114 site of one connexin. For the sodium and potassium simulations, no specific interactions with the protein were found. Altogether, these results suggest that mass and steric effects play an important role in determining cation binding to Cx26 hemichannels.

更新日期：2019-07-20

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