Vicinal disulfide turns
Vicinal disulfide turns
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DOI：
10.1093/protein/gzg088
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发表时间：
2003-09-01
期刊：
影响因子：
--
通讯作者：
Pongor, S
中科院分区：
文献类型：
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作者：
Carugo, O;Cemazar, M;Pongor, S
相邻半胱氨酸残基之间的二硫键的形成伴随着蛋白质骨架的紧致转折的形成。在分析的近90%的结构中，发现了VIII型转弯。两个半胱氨酸之间的肽键为扭曲的反式构象，omega扭转角在159~-133度之间，平均值为171度。邻位二硫键转折的受限性质以及在氧化和还原状态之间观察到的显著差异，表明邻位二硫键可能被用作“氧化还原激活的”构象开关。
The formation of a disulfide bond between adjacent cysteine residues is accompanied by the formation of a tight turn of the protein backbone. In nearly 90% of the structures analyzed a type VIII turn was found. The peptide bond between the two cysteines is in a distorted trans conformation, the omega torsion angle ranges from 159 to -133degrees, with an average value of 171degrees. The constrained nature of the vicinal disulfide turn and the pronounced difference observed between the oxidized and reduced states, suggests that vicinal disulfides may be employed as a 'redox-activated' conformational switch.