FK506 Binding Proteins (FKBPs) are a family of highly conserved and important proteins that possess a peptidyl cis–trans isomerase (PPIases) domain. Human FKBP12 is a prototype of this family and it is involved in many diseases due to its interaction with the immunosuppressive drugs FK506 and rapamycin. They inhibit calcineurin and mTOR complex, respectively, leading to parasite death by inhibiting cell proliferation through cytokinesis blockade being an important target to find new drugs. Tuberculosis is a disease that causes important impacts on public health worldwide. In this context, MtFKBP12 is a putative peptidyl prolyl cis–trans isomerase from Mycobacterium tuberculosis and here we report the NMR chemical shift assignment for ¹H, ¹⁵N and ¹³C nuclei in the backbone and side chains of the MtFKBP12. This lays the foundation for further structural studies, backbone dynamics, mapping of interactions and drug screening and development. We have found through the NMR spectrum that the protein is well folded with narrow peaks and almost none overlap in ¹⁵N-HSQC. Prediction of secondary structure using Talos-N server showed great similarity with other proteins from this family.

中文翻译：

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来自结核分枝杆菌的推定肽基脯氨酰顺反异构酶 FKBP12 的主链和侧链 1H、15N 和 13C 分配。

FK506 结合蛋白 (FKBPs) 是一个高度保守且重要的蛋白质家族，具有肽基顺反异构酶 (PPIases) 结构域。人 FKBP12 是该家族的原型，由于它与免疫抑制药物 FK506 和雷帕霉素相互作用，因此涉及许多疾病。它们分别抑制钙调神经磷酸酶和 mTOR 复合物，通过胞质分裂阻断抑制细胞增殖来导致寄生虫死亡，这是寻找新药的重要目标。结核病是一种对全世界公共卫生造成重要影响的疾病。在这种情况下，MtFKBP12 是一种来自结核分枝杆菌的推定肽基脯氨酰顺反异构酶，在这里我们报告了¹MtFKBP12 的主链和侧链中的H、¹⁵ N 和¹³ C 核。这为进一步的结构研究、骨架动力学、相互作用图谱以及药物筛选和开发奠定了基础。我们通过 NMR 谱发现，蛋白质折叠良好，峰很窄，在¹⁵ N-HSQC 中几乎没有重叠。使用 Talos-N 服务器的二级结构预测显示与该家族的其他蛋白质有很大的相似性。