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首页> 外文期刊>Dalton transactions: An international journal of inorganic chemistry >A comparative study on the possible zinc binding sites of the human ZnT3 zinc transporter protein
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A comparative study on the possible zinc binding sites of the human ZnT3 zinc transporter protein

机译：人ZnT3锌转运蛋白可能的锌结合位点的比较研究

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摘要

The brain specific zinc transporter protein ZnT3 can be related to the amyloid neuropathology of Alzheimer's disease. In order to analyze the metal binding ability of human ZnT3 protein, here we report a potentiometric and solution structural (UV-Vis, CD, EPR, NMR) study of nickel(ii), copper(ii) and zinc(ii) complexes of three peptides mimicking the possible metal binding sequences of this protein. The peptide L~1 (Ac-RHQAGPPHSHR-NH _2) is a minimalist, the cyclic peptide L~2 (cyclo(Ac-CKLHQAGPPHSHGSRGAEYAPLEEGPEEKC-NH_2) is a more complete model of the intracellular His-rich loop, which is widely accepted as a putative metal binding site. The peptide L~3 (Ac-PFHHCHRD-NH_2) is the model of the conserved cytoplasmic N-terminal -HHCH- sequence. In the physiological pH-range, the ZnL~1, ZnH_3L~2 and ZnL~3 complexes are the major species in the corresponding binary systems, with &8b;3Nim&8f;, &8b;3N_(im),2/3O_(amide)&8f; and &8b;3N_(im),S~-&8f; coordination environments, respectively. The species ZnL~3 has 3-4 orders of magnitude higher stability than the other two complexes, indicating the presence of a high-affinity zinc-binding site at the N-terminal tail of the human ZnT3 transporter. Moreover, L ~3 shows preferred zinc binding as compared to nickel (log β(ZnL~3) - log β(NiL~3) = 2.3), probably due to the higher preference of zinc(ii) for tetrahedral geometry. These facts suggest that zinc binding to the N-terminal -HHCH- sequence of human ZnT3 may be involved in the biological activity of this zinc transporter protein in zinc sensing, binding or translocation processes.
机译：脑特异性锌转运蛋白ZnT3可能与阿尔茨海默氏病的淀粉样蛋白神经病理学有关。为了分析人ZnT3蛋白的金属结合能力，在这里我们报告了镍（ii），铜（ii）和锌（ii）配合物的电位和溶液结构（UV-Vis，CD，EPR，NMR）研究。模仿该蛋白质可能的金属结合序列的三个肽。肽L〜1（Ac-RHQAGPPHSHR-NH _2）是极简主义者，环肽L〜2（cyclo（Ac-CKLHQAGPPHSHGSRGAEYAPLEEGPEEKC-NH_2）是细胞内His-rich环的更完整模型，被广泛接受为L〜3（Ac-PFHHCHRD-NH_2）肽是保守的细胞质N端-HHCH-序列的模型，在生理pH范围内，ZnL〜1，ZnH_3L〜2和ZnL 〜3络合物是相应二元系统中的主要种类，具有＆8b; 3Nim＆8f;，＆8b; 3N_（im），2 / 3O_（酰胺）＆8f;和＆8b; 3N_（im），S〜-＆8f;协调环境， ZnL〜3物种的稳定性比其他两种复合物高3-4个数量级，表明在人类ZnT3转运蛋白的N末端尾部存在高亲和力的锌结合位点。图3显示了与镍相比更好的锌结合（logβ（ZnL〜3）-logβ（NiL〜3）= 2.3），这可能是由于锌（ii）对四面体几何形状的偏爱更高。锌与人ZnT3的N端-HHCH-序列的结合可能与锌转运蛋白在锌感测，结合或转运过程中的生物活性有关。

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