{Reference Type}: Journal Article
{Title}: Location of S-nitrosylated cysteines in protein three-dimensional structures.
{Author}: Carugo O;
{Journal}: Proteins
{Volume}: 92
{Issue}: 4
{Year}: 2024 Apr 8
{Factor}: 4.088
{DOI}: 10.1002/prot.26629
{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.