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PMID: 15582391 Published · ppublish English Journal Article Review

The role of cysteine residues as redox-sensitive regulatory switches.

Current opinion in structural biology ·Vol. 14 ·No. 6 ·2004-12-00 ·Pages 679-86

Barford D

Abstract

Redox-sensitive cysteine residues sense and transduce changes in cellular redox status caused by the generation of reactive oxygen species and the presence of oxidised thiols. Oxidation of such cysteines is converted into signals that control cell regulatory pathways and induction of gene expression. A variety of proteins, including transcription factors, molecular chaperones and protein tyrosine phosphatases, are regulated via redox processes. Common mechanisms underlie the sensitivity of cysteines to redox, such as proximity to polar and charged groups, and signal transduction is exerted via conformational changes that are conferred by the formation of disulfide and cyclic sulfenamide covalent bonds, and sulfenic and sulfonic acids.

MeSH Terms
Animals Binding Sites Catalysis Cysteine/chemistry,metabolism Gene Expression Regulation/physiology Humans Models, Biological Models, Chemical Models, Molecular Oxidation-Reduction Oxidative Stress/physiology Protein Binding Protein Conformation Signal Transduction/physiology Structure-Activity Relationship
Chemicals
Cysteine
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Barford David
Section of Structural Biology, Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, London SW3 6JB, UK. [email protected]
Article Info
Journal
Current opinion in structural biology
Abbr.
Curr Opin Struct Biol
ISSN
0959-440X
Published
2004-12-00
Pages
679-86
Language
English
Region
England
NLM ID
9107784
Subset
IM
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