Zinc-Binding Cysteines: Diverse Functions and Structural Motifs

By N. Pace, E. Weerapana. 2014

211 citations recorded by the source corpus.

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.

Subfields: Molecular Biology, Nutrition and Dietetics

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

In Nutrition and Dietetics

Citations in the corpus

IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding (2018, background): “However, they can also play essential roles in stabilizing the folded conformation by coordinating Zn 2+ ions under reducing conditions, or by forming disulfide bonds that are commonly used by extracellular proteins that experience oxidative conditions (46).”
Antioxidant and anti-inflammatory effects of zinc. Zinc-dependent NF-κB signaling (2017, background): “Other examples of sulfhydryl-containing proteins protected by zinc are DNA zinc-binding proteins (zinc fingers), alanyl tRNA synthetase, tubulin, and dihydroorotase (Mocchegiani et al. 2000; Rink and Gabriel 2001; Pace and Weerapana 2014).”