S-亚硝化半胱氨酸在蛋白质三维结构中的定位。

IF 4.3 3区 材料科学 Q1 ENGINEERING, ELECTRICAL & ELECTRONIC
ACS Applied Electronic Materials Pub Date : 2024-04-01 Epub Date: 2023-11-08 DOI:10.1002/prot.26629
Oliviero Carugo
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引用次数: 0

摘要

尽管半胱氨酸的S-亚硝基化是一种常见的蛋白质翻译后修饰,但对其三维结构特征知之甚少。本文描述了对蛋白质数据库中可用数据的系统调查。可以提出一些有趣的意见。(1) 由于辐射损伤,S-亚硝化半胱氨酸(Snc)经常被减少,至少部分减少。(2) S-亚硝基化可能是对不可逆硫醇氧化的保护;由于Snc的NO基团对溶剂是相对可接近的,它可以充当软木塞来保护半胱氨酸的硫原子不被分子氧氧化为亚磺、亚磺和磺酸;此外,Snc经常出现在螺旋和股线的开始或结束处,这可能会阻止二级结构元件的展开。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Location of S-nitrosylated cysteines in protein three-dimensional structures.

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.

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来源期刊
CiteScore
7.20
自引率
4.30%
发文量
567
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