Zinc-binding cysteines: diverse functions and structural motifs.
Zinc-binding cysteines: diverse functions and structural motifs.
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DOI：
10.3390/biom4020419
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发表时间：
2014-04-17
期刊：
影响因子：
5.5
通讯作者：
Weerapana E
中科院分区：
文献类型：
--
作者：
Pace NJ;Weerapana E
已知半胱氨酸残基在蛋白质中具有重要功能，包括与各种金属离子结合。尤其是半胱氨酸残基对锌离子(锌离子)具有很高的亲和力，这些锌离子-半胱氨酸络合物是蛋白质结构、催化和调控的关键介质。最近在实验和理论平台上的进展加速了锌结合半胱氨酸的鉴定和功能表征。锌-半胱氨酸复合体已经在不同的蛋白质类别中被观察到，并被认为促进了各种细胞过程。在这里，我们重点介绍了蛋白质中锌离子-半胱氨酸复合体的结构特征和不同的功能作用，并描述了结构、计算和化学蛋白质组学技术，这些技术使全球能够发现与锌离子结合的新型半胱氨酸。
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.