National Tsing Hua University, Chemistry Department, Hsinchu, Taiwan.
Graduate Institute of Biomedical Sciences and Center for Molecular Medicine, China Medical University, Taichung, Taiwan.
PLoS One. 2019 Feb 19;14(2):e0212299. doi: 10.1371/journal.pone.0212299. eCollection 2019.
The Ca2+-dependent human S100A4 (Mts1) protein is part of the S100 family. Here, we studied the interactions of S100A4 with S100A1 using nuclear magnetic resonance (NMR) spectroscopy. We used the chemical shift perturbed residues from HSQC to model S100A4 and S100A1 complex with HADDOCK software. We observed that S100A1 and the RAGE V domain have an analogous binding area in S100A4. We discovered that S100A4 acts as an antagonist among the RAGE V domain and S100A1, which inhibits tumorigenesis and cell proliferation. We used a WST-1 assay to examine the bioactivity of S100A1 and S100A4. This study could possibly be beneficial for evaluating new proteins for the treatment of diseases.
依赖 Ca2+的人 S100A4（Mts1）蛋白是 S100 家族的一部分。在这里，我们使用核磁共振（NMR）光谱研究了 S100A4 与 S100A1 之间的相互作用。我们使用 HSQC 中的化学位移扰动残基来使用 HADDOCK 软件对 S100A4 和 S100A1 复合物进行建模。我们观察到 S100A1 和 RAGE V 结构域在 S100A4 中有类似的结合区域。我们发现 S100A4 作为 RAGE V 结构域和 S100A1 之间的拮抗剂，抑制肿瘤发生和细胞增殖。我们使用 WST-1 测定法检查了 S100A1 和 S100A4 的生物活性。这项研究对于评估治疗疾病的新蛋白质可能是有益的。
