Department of Chemistry, University of Pavia, Pavia, Italy.
Protein Pept Lett. 2020;27(8):763-769. doi: 10.2174/0929866527666200305144447.
Despite the fact that lithium is not a biologically essential metallic element, its pharmacological properties are well known and human exposure to lithium is increasingly possible because of its used in aerospace industry and in batteries.
Lithium-protein interactions are therefore interesting and the surveys of the structures of lithium-protein complexes is described in this paper.
A high quality non-redundant set of lithium containing protein crystal structures was extracted from the Protein Data Bank and the stereochemistry of the lithium first coordination sphere was examined in detail.
Four main observations were reported: (i) lithium interacts preferably with oxygen atoms; (ii) preferably with side-chain atoms; (iii) preferably with Asp or Glu carboxylates; (iv) the coordination number tends to be four with stereochemical parameters similar to those observed in small molecules containing lithium.
Although structural information on lithium-protein, available from the Protein Data Bank, is relatively scarce, these trends appears to be so clear that one may suppose that they will be confirmed by further data that will join the Protein Data Bank in the future.
尽管锂不是一种生物必需的金属元素，但它的药理学性质是众所周知的，而且由于其在航空航天工业和电池中的应用，人类接触锂的可能性越来越大。
因此，锂-蛋白质相互作用是有趣的，本文描述了锂-蛋白质复合物的结构研究。
从蛋白质数据库中提取了高质量的、非冗余的含锂蛋白质晶体结构数据集，并详细检查了锂的第一配位层的立体化学。
报告了四个主要观察结果：（i）锂优先与氧原子相互作用；（ii）优先与侧链原子相互作用；（iii）优先与 Asp 或 Glu 羧酸根相互作用；（iv）配位数倾向于四，立体化学参数与含有锂的小分子中观察到的相似。
尽管从蛋白质数据库中获得的关于锂-蛋白质的结构信息相对较少，但这些趋势似乎非常明显，因此可以假设，随着未来更多数据加入蛋白质数据库，这些趋势将得到进一步证实。
