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Biomolecules 2014, 4(2), 419-434; doi:10.3390/biom4020419

Zinc-Binding Cysteines: Diverse Functions and Structural Motifs

Department of Chemistry, Boston College, 2609 Beacon Street, Chestnut Hill, MA 02467, USA
* Author to whom correspondence should be addressed.
Received: 6 February 2014 / Revised: 19 March 2014 / Accepted: 20 March 2014 / Published: 17 April 2014
(This article belongs to the Special Issue Metal Binding Proteins)
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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.
Keywords: zinc; cysteine; zinc-cysteine complexes; zinc fingers; zinc inhibition; regulatory zinc zinc; cysteine; zinc-cysteine complexes; zinc fingers; zinc inhibition; regulatory zinc
This is an open access article distributed under the Creative Commons Attribution License (CC BY) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Pace, N.J.; Weerapana, E. Zinc-Binding Cysteines: Diverse Functions and Structural Motifs. Biomolecules 2014, 4, 419-434.

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