Pace Nicholas J, Weerapana Eranthie
Department of Chemistry, Boston College, 2609 Beacon Street, Chestnut Hill, MA 02467, USA.
Biomolecules. 2014 Apr 17;4(2):419-34. doi: 10.3390/biom4020419.
Cysteine residues are known to perform essential functions within proteins, including binding to various metal ions. In particular, cysteine residues can display high affinity toward zinc ions (Zn2+), and these resulting Zn2+-cysteine complexes are critical mediators of protein structure, catalysis and regulation. Recent advances in both experimental and theoretical platforms have accelerated the identification and functional characterization of Zn2+-bound cysteines. Zn2+-cysteine complexes have been observed across diverse protein classes and are known to facilitate a variety of cellular processes. Here, we highlight the structural characteristics and diverse functional roles of Zn2+-cysteine complexes in proteins and describe structural, computational and chemical proteomic technologies that have enabled the global discovery of novel Zn2+-binding cysteines.
半胱氨酸残基在蛋白质中发挥着重要功能，包括与各种金属离子结合。特别是，半胱氨酸残基对锌离子（Zn2+）具有高亲和力，这些形成的Zn2+-半胱氨酸复合物是蛋白质结构、催化和调节的关键介质。实验和理论平台的最新进展加速了与锌结合的半胱氨酸的鉴定和功能表征。在各种蛋白质类别中都观察到了Zn2+-半胱氨酸复合物，并且已知它们促进多种细胞过程。在这里，我们强调了蛋白质中Zn2+-半胱氨酸复合物的结构特征和多样的功能作用，并描述了能够在全球范围内发现新型锌结合半胱氨酸的结构、计算和化学蛋白质组学技术。
