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Biomolecules. 2014 Apr 17;4(2):419-34. doi: 10.3390/biom4020419.

Zinc-binding cysteines: diverse functions and structural motifs.

Author information

1
Department of Chemistry, Boston College, 2609 Beacon Street, Chestnut Hill, MA 02467, USA. nicholas.pace@bc.edu.
2
Department of Chemistry, Boston College, 2609 Beacon Street, Chestnut Hill, MA 02467, USA. eranthie.weerapana@bc.edu.

Abstract

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.

PMID:
24970223
PMCID:
PMC4101490
DOI:
10.3390/biom4020419
[Indexed for MEDLINE]
Free PMC Article
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