Zinc-binding cysteines: diverse functions and structural motifs

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...

Full description

Saved in:
Bibliographic Details
Published in:Biomolecules (Basel, Switzerland) Switzerland), 2014-04, Vol.4 (2), p.419-434
Main Authors: Pace, Nicholas J, Weerapana, Eranthie
Format: Article
Language:English
Subjects:
Animals
Biological Transport
cysteine
Cysteine - metabolism
Humans
Proteins - chemistry
Proteins - metabolism
regulatory zinc
Review
zinc
Zinc - metabolism
Zinc Fingers
zinc inhibition
zinc-cysteine complexes
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:2218-273X
2218-273X
DOI:10.3390/biom4020419