[血清白蛋白:根据分子建模数据寻找具有酯酶活性的新位点]。

Bioorganicheskaia khimiia Pub Date : 2014-09-01
D A Belinskaia, V I Shmurak, D S Prokof'eva, N V Goncharov
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引用次数: 0

摘要

众所周知,白蛋白能够切断有机磷酸酯(OPs)中的酯键。负责白蛋白对OPs的酯酶和伪酯酶活性的氨基酸仍未确定。本研究的目的是利用分子模拟方法,以白蛋白与人体相互作用为例,确定其酯酶活性的潜在位点。采用分子对接方法确定了与索曼蛋白配合物的结构,并用分子动力学方法模拟了配合物的稳定性。已经确定,只有在酪氨酸去质子化之后,才有可能在Tyr411附近产生索曼吸附。Tyr150比Tyr411更有效地结合人体;Tyr150的去质子化不影响结合效率,但影响配合物的稳定性。提出了与人有关的白蛋白Tyr150的真酯酶活性。结果表明,Ser193也可能与白蛋白的酯酶活性有关。我们假设其中一个位点的催化氨基酸的去质子化可以由其他位点的配体结合(变构调节)引发。
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[Serum albumin: search for new sites with esterase activity according to molecular modeling data].

It is known that albumin is able to cut ester bonds in organophosphates (OPs). Amino acids responsible for esterase and pseudo-esterase activity of albumin towards OPs are still not determined. The purpose of this study is to identify the potential sites of esterase activity of albumin by the example of its interaction with soman using molecular modeling methods. The structures of the protein complexes with soman was determined by molecular docking procedure, the stability of the complexes were simulated using molecular dynamics method. It has been determined that productive sorption of soman near Tyr411 is possible only after deprotonation of the tyrosine. Tyr150 binds soman more efficiently than Tyr411; deprotonation of Tyr150 does not affect the binding efficiency, but affects on the stability of the complexes. The true esterase activity of albumin Tyr150 in relation to soman is proposed. It is shown that Ser193 can also be responsible for the esterase activity of albumin. We hypothesize that deprotonation of catalytic amino acid in one of the sites could be initiated by ligand binding in other sites (allosteric regulation).

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