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首页> 外文期刊>Biochemistry >Elucidation of Inositol Hexaphosphate and Heparin Interaction Sites and Conformational Changes in Arrestin-1 by Solution Nuclear Magnetic Resonance
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Elucidation of Inositol Hexaphosphate and Heparin Interaction Sites and Conformational Changes in Arrestin-1 by Solution Nuclear Magnetic Resonance

机译：溶液核磁共振阐明六磷酸肌醇与肝素的相互作用位点和Arrestin-1的构象变化

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摘要

Arrestins specifically bind activated and phosphorylated G protein-coupled receptors andnorchestrate both receptor trafficking and channel signaling through G protein-independent pathways viandirect interactions with numerous nonreceptor partners. Here we report the first successful use of solutionnNMR in mapping the binding sites in arrestin-1 (visual arrestin) for two polyanionic compounds that mimicnphosphorylated light-activated rhodopsin: inositol hexaphosphate (IP6) and heparin. This yielded annidentification of residues involved in the binding with these ligands that was more complete than what hasnpreviously been feasible. IP6 and heparin appear to bind to the same site on arrestin-1, centered on a positivelyncharged region in the N-domain. We present the first direct evidence that both IP6 and heparin induced ancomplete release of the arrestin C-tail. These observations provide novel insight into the nature of thentransition of arrestin from the basal to active state and demonstrate the potential of NMR-based methods innthe study of protein-protein interactions involving members of the arrestin family.
机译：抑制蛋白特异性结合活化的和磷酸化的G蛋白偶联受体，并通过与G蛋白非依赖性途径与许多非受体伴侣的直接相互作用来阻断受体运输和通道信号传导。在这里，我们报道了首次成功使用solutionnNMR绘制了抑制素1（视觉抑制素）中两个模仿磷酸化光激活视紫红质的聚阴离子化合物的结合位点：肌醇六磷酸（IP6）和肝素。这样就鉴定了与这些配体结合所涉及的残基，该残基比以前可行的残基更完整。 IP6和肝素似乎结合在抑制蛋白1上的同一位点上，中心位于N结构域的带正电荷的区域。我们目前提供的第一个直接证据表明IP6和肝素都诱导了逮捕素C尾巴的完全释放。这些观察结果提供了新的洞察力，将抑制蛋白从基础状态转变为活性状态，并证明了基于核磁共振的方法在涉及抑制蛋白家族成员的蛋白质相互作用研究中的潜力。

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