In the body, extracellular stimuli produce inositol 1,4,5-trisphosphate (IP3), an intracellular chemical signal that binds to the IP3 receptor (IP3R) to release calcium ions (Ca2+) from the endoplasmic reticulum. In the past 40 years, the wide-ranging functions mediated by IP3R and its genetic defects causing a variety of disorders have been unveiled. Recent cryo-electron microscopy and X-ray crystallography have resolved IP3R structures and begun to integrate with concurrent functional studies, which can explicate IP3-dependent opening of Ca2+-conducting gates placed ∼90 Å away from IP3-binding sites and its regulation by Ca2+. This review highlights recent research progress on the IP3R structure and function. We also propose how protein plasticity within IP3R, which involves allosteric gating and assembly transformations accompanied by rapid and chronic structural changes, would enable it to regulate diverse functions at cellular microdomains in pathophysiological states.

中文翻译：

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多种功能背后的IP3受体可塑性。

在体内，细胞外刺激产生肌醇1,4,5-三磷酸（IP3），这是一种细胞内化学信号，与IP3受体（IP3R）结合，从内质网释放钙离子（Ca2 +）。在过去的40年中，由IP3R介导的广泛功能及其导致多种疾病的遗传缺陷被揭示出来。最近的低温电子显微镜和X射线晶体学已经解决了IP3R的结构问题，并开始与并行的功能研究相结合，可以阐明IP3依赖的Ca2 +传导门的开路，距离IP3结合位点约90Å，并且受Ca2 +的调节。这篇综述重点介绍了IP3R结构和功能的最新研究进展。我们还提出了IP3R中蛋白质可塑性的方法，