title: Zinc-binding cysteines: diverse functions and structural motifs.
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.
authors: Department of Chemistry, Boston College, 2609 Beacon Street, Chestnut Hill, MA 02467, USA. nicholas.pace@bc.edu.
authors: Nicholas J
authors: NJ
authors: Pace
authors: Department of Chemistry, Boston College, 2609 Beacon Street, Chestnut Hill, MA 02467, USA. eranthie.weerapana@bc.edu.
authors: Eranthie
authors: E
authors: Weerapana
mesh_terms: D000818:Animals; D001692:Biological Transport; D003545:Cysteine / Q000378:metabolism*; D006801:Humans; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D015032:Zinc / Q000378:metabolism*; D016335:Zinc Fingers
chemical_list: D011506:Proteins; D015032:Zinc; D003545:Cysteine