PDF(Pubmed)
Abstract：
Human serum albumin (HSA) is the most abundant plasma protein, which functions to transport a large range of ligands within the circulation. These interactions have important implications for human health and disease. The primary binding site for CuII ions on HSA is known to be the so-called amino-terminal CuII and NiII binding (ATCUN) motif. However, the number and identity of secondary binding sites is currently not understood. In this study, we harnessed a suite of contemporary electron paramagnetic resonance (EPR) spectroscopy methods to investigate recombinantly produced constructs of HSA bearing single-histidine knockouts, with the aim to characterise its endogenous CuII ion binding sites.
摘要：
人血清白蛋白(HSA)是最丰富的血浆蛋白,其功能是在循环中运输大范围的配体。这些相互作用对人类健康和疾病具有重要意义。已知CuII离子在HSA上的主要结合位点是所谓的氨基末端CuII和NiII结合(ATCUN)基序。然而,目前尚不了解二级结合位点的数量和身份。在这项研究中,我们利用了一套当代电子顺磁共振（EPR）光谱方法来研究重组产生的HSA携带单组氨酸敲除的构建体，目的是表征其内源性CuII离子结合位点。
