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Location of S‐nitrosylated cysteines in protein three‐dimensional structures.
- Source :
- Proteins; Apr2024, Vol. 92 Issue 4, p464-473, 10p
- Publication Year :
- 2024
-
Abstract
- Although S‐nitrosylation of cysteines is a common protein posttranslational modification, little is known about its three‐dimensional structural features. This paper describes a systematic survey of the data available in the Protein Data Bank. Several interesting observations could be made. (1) As a result of radiation damage, S‐nitrosylated cysteines (Snc) are frequently reduced, at least partially. (2) S‐nitrosylation may be a protection against irreversible thiol oxidation; because the NO group of Snc is relatively accessible to the solvent, it may act as a cork to protect the sulfur atoms of cysteines from oxidation by molecular oxygen to sulfenic, sulfinic, and sulfonic acid; moreover, Snc are frequently found at the start or end of helices and strands and this might shield secondary structural elements from unfolding. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 08873585
- Volume :
- 92
- Issue :
- 4
- Database :
- Complementary Index
- Journal :
- Proteins
- Publication Type :
- Academic Journal
- Accession number :
- 175918627
- Full Text :
- https://doi.org/10.1002/prot.26629