在细胞中，Lanmodulin 保持未折叠状态，无法与镧系元素离子相互作用。
Lanmodulin remains unfolded and fails to interact with lanthanide ions in cells.
机构信息
Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan National Laboratory for Optoelectronics, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan, 430071, China.
Graduate University of Chinese Academy of Sciences, Beijing, 100049, China.
出版信息
Chem Commun (Camb). 2022 Jul 21;58(59):8230-8233. doi: 10.1039/d2cc02038f.
We report the conformation of a newly discovered specific lanthanide ion (Ln) binding protein, lanmodulin (LanM), and its interaction with Ln in cells using the in-cell NMR technique. We found that LanM remains unfolded and fails to bind Ln in cells due to the abundance of phosphate groups.
我们报道了一种新发现的特定镧系离子（Ln）结合蛋白——lanmodulin（LanM）的构象，并使用细胞内 NMR 技术研究了其在细胞内与 Ln 的相互作用。我们发现由于磷酸盐基团的丰富，LanM 在细胞内仍然处于未折叠状态，无法与 Ln 结合。
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