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首页> 外文期刊>Applied Magnetic Resonance >Cu(II) EPR Reveals Two Distinct Binding Sites and Oligomerization of Innate Immune Protein Calgranulin C
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Cu(II) EPR Reveals Two Distinct Binding Sites and Oligomerization of Innate Immune Protein Calgranulin C

机译：Cu（ii）epr揭示了两个不同的结合位点和先天免疫蛋白Calgranulin c的寡聚化

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S100A12 or Calgranulin C is a homodimeric antimicrobial protein of the S100 family of EF-hand calcium-modulated proteins. S100A12 is involved in many diseases such as inflammation, tumor invasion, cancer and neurological disorders such as Alzheimer’s disease. The binding of transition metal ions to the protein is important as the sequestering of the metal ion induces conformational changes in the protein, inhibiting the growth of various pathogenic microorganisms. In this work, we probe the Cu_(2+)binding properties of Calgranulin C. We demonstrate that the two Cu_(2+)binding sites in Calgranulin C show different coordination environments in solution. Continuous wave-electron spin resonance?(CW-ESR) spectra of Cu_(2+)-bound protein clearly show two distinct components at higher Cu_(2+):protein ratios, which is indicative of the two different binding environments for the Cu_(2+)ions. The g~(||)and A~(||)values are also different for the two components, indicating that the number of directly coordinated nitrogen in each site differs. Furthermore, we perform CW-ESR titrations to obtain the binding affinity of the Ca_(2+)-loaded protein to Cu_(2+)ions. We observe a positive cooperativity in binding of the two Cu_(2+)ions. To further probe the Cu_(2+)coordination, we also perform electron spin echo envelope modulation (ESEEM) experiment. We perform ESEEM at two different fields where one Cu_(2+)binding site dominates the other. At both sites we see distinct signatures of Cu_(2+)–histidine coordination. However, we clearly see that the ESEEM spectra corresponding to the two Cu_(2+)binding sites are significantly different. There is clear change in the intensity of the double quantum peak with respect to the nuclear quadrupole interaction peak at the two different fields. Furthermore, ESEEM along with hyperfine sublevel correlation show that only one of the two Cu_(2+)binding sites has backbone coordination, confirming our previous observation. Finally, we perform double
机译：S100A12或Calgranulin C是S100的EF-Hand钙调制蛋白的同型抗微生物蛋白。 S100A12涉及许多疾病，如炎症，肿瘤侵袭，癌症和神经系统疾病，如阿尔茨海默病。过渡金属离子与蛋白质的结合是因为金属离子的螯合诱导蛋白质中的构象变化，抑制各种病原微生物的生长。在这项工作中，我们探测CALGRANULIN C的CU_（2+）结合性质。我们证明CALGRANULIN C中的两个CU_（2+）结合位点在溶液中显示出不同的协调环境。 Cu_（2 +）结合蛋白的连续波 - 电子旋转共振α（CW-ESR）光谱在较高Cu_（2 +）：蛋白质比下清楚地显示出两个不同的组分，其表示CU_的两个不同的绑定环境（2+）离子。对于两个组分，G〜（||）和〜（||）值也不同，表明每个部位在每个部位的直接协调氮的数量不同。此外，我们进行CW-ESR滴定，以获得Ca_（2 +） - 负载蛋白对Cu_（2+）离子的结合亲和力。我们观察到两个Cu_（2+）离子的结合的正合作性。为了进一步探测Cu_（2+）的协调，我们还执行电子旋转回波包络调制（ESEEM）实验。我们在两个不同的领域执行ESEEM，其中一个CU_（2+）绑定站点占据另一个。在两个网站中，我们看到Cu_（2 +） - 组氨酸的不同签名。然而，我们清楚地看到，对应于两个Cu_（2+）结合位点的ESEEM光谱显着不同。双量子峰的强度有明显的改变两种不同领域的核Quadrupole相互作用峰值。此外，Eseem以及Hyperfine Sublevel相关性表明，只有两个Cu_（2+）结合位点中只有一个具有骨干协调，确认我们之前的观察。最后，我们进行双重

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