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首页> 外文期刊>Acta crystallographica. Section D, Structural biology. >The X‐ray structure of human calbindin‐D28K: an improved model
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The X‐ray structure of human calbindin‐D28K: an improved model

机译：人类calbindin D28K应承担的X射线应承担的结构:一个改进的模型

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摘要

Calbindin‐D28K is a widely expressed calcium‐buffering cytoplasmic protein that is involved in many physiological processes. It has been shown to interact with other proteins, suggesting a role as a calcium sensor. Many of the targets of calbindin‐D28K are of therapeutic interest: for example, inositol monophosphatase, the putative target of lithium therapy in bipolar disorder. Presented here is the first crystal structure of human calbindin‐D28K. There are significant deviations in the tertiary structure when compared with the NMR structure of rat calbindin‐D28K (PDB entry 2g9b ), despite 98% sequence identity. Small‐angle X‐ray scattering (SAXS) indicates that the crystal structure better predicts the properties of calbindin‐D28K in solution compared with the NMR structure. Here, the first direct visualization of the calcium‐binding properties of calbindin‐D28K is presented. Four of the six EF‐hands that make up the secondary structure of the protein contain a calcium‐binding site. Two distinct conformations of the N‐terminal EF‐hand calcium‐binding site were identified using long‐wavelength calcium single‐wavelength anomalous dispersion (SAD). This flexible region has previously been recognized as?a protein–protein interaction interface. SAXS data collected in both the presence and absence of calcium indicate that there are no large structural differences in the globular structure of calbindin‐D28K between the calcium‐loaded and unloaded proteins.
机译：Calbindin D28K应承担的是一种广泛表达钙量缓冲细胞质蛋白质参与了许多生理过程。被证明与其他蛋白质相互作用,建议作为钙传感器。的目标calbindin D28K应承担的治疗兴趣:例如,肌醇monophosphatase,锂治疗双相的假定的目标障碍。人类calbindin D28K应承担的结构。三级结构的重大偏差与老鼠的NMR结构相比calbindin D28K应承担(PDB项2 g9b),尽管98%序列的身份。(粉煤灰)表明,晶体结构更好的预测calbindin D28K应承担的属性在溶液中与NMR结构。这里,第一个直接可视化钙量calbindin D28K应承担的绑定属性提出了。蛋白质的二级结构包含一个钙的结合位点。N量的终端EF手应承担的钙结合位点确定了使用长期波长钙单波长反常色散(SAD)。这曾被灵活的区域认为是吗?接口。表明存在和缺乏钙没有大的结构性差异之间的calbindin D28K应承担的球状结构钙量蛋白质加载和卸载。

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