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首页> 外文期刊>Journal of Molecular Biology >A Neutral Molecule in a Cation-binding Site: Specific Binding of a PEG-SH to Acetylcholinesterase from Torpedo californica.
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A Neutral Molecule in a Cation-binding Site: Specific Binding of a PEG-SH to Acetylcholinesterase from Torpedo californica.

机译：阳离子结合位点的中性分子：PEG-SH与来自加州鱼雷的乙酰胆碱酯酶的特异性结合。

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摘要

The crystal structure of acetylcholinesterase from Torpedo californica complexed with the uncharged inhibitor, PEG-SH-350 (containing mainly heptameric polyethylene glycol with a terminal thiol group) is determined at 2.3 A resolution. This is an untypical acetylcholinesterase inhibitor, since it lacks the cationic moiety typical of the substrate (acetylcholine). In the crystal structure, the elongated ligand extends along the whole of the deep and narrow active-site gorge, with the terminal thiol group bound near the bottom, close to the catalytic site. Unexpectedly, the cation-binding site (formed by the faces of aromatic side-chains) is occupied by CH(2) groups of the inhibitor, which are engaged in C-Hcdots, three dots, centeredpi interactions that structurally mimic the cation-pi interactions made by the choline moiety of acetylcholine. In addition, the PEG-SH molecule makes numerous other weak but specific interactions of the C-Hcdots, three dots, centeredO and C-Hcdots, three dots, centeredpi types. (c) 2002 Elsevier Science Ltd.
机译：以2.3 A的分辨率测定来自Torpedo californica的乙酰胆碱酯酶与不带电荷的抑制剂PEG-SH-350（主要包含具有末端硫醇基的七聚乙二醇）复合的晶体结构。这是一种非典型的乙酰胆碱酯酶抑制剂，因为它缺乏典型的底物阳离子部分（乙酰胆碱）。在晶体结构中，细长的配体沿着整个深而窄的活性位点峡谷延伸，末端硫醇基团结合在底部附近，靠近催化位点。出乎意料的是，阳离子结合位点（由芳香族侧链的表面形成）被抑制剂的CH（2）组占据，它们参与C-Hcdots，三个点，centeredpi相互作用，在结构上模拟阳离子-pi乙酰胆碱的胆碱部分产生的相互作用。此外，PEG-SH分子使C-Hcdots，三个点，centeredO和C-Hcdots，三个点，centeredpi类型发生了许多其他弱但特异的相互作用。 （c）2002爱思唯尔科学有限公司。

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