Journal
BIOMOLECULES
Volume 4, Issue 2, Pages 419-434Publisher
MDPI
DOI: 10.3390/biom4020419
Keywords
zinc; cysteine; zinc-cysteine complexes; zinc fingers; zinc inhibition; regulatory zinc
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Funding
- Damon Runyon Cancer Foundation [DRR-18-12]
- Smith Family Foundation
- Boston College
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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.
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