On methylene-bridged cysteine and lysine residues in proteins.
On methylene-bridged cysteine and lysine residues in proteins.
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关于蛋白质中亚甲基桥半胱氨酸和赖氨酸残基。
DOI：
10.1002/pro.2958
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发表时间：
2016
期刊：
影响因子：
--
通讯作者：
Dauter,Zbigniew
中科院分区：
文献类型：
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作者：
Ruszkowski,Milosz;Dauter,Zbigniew
半胱氨酸残基通过形成二硫键来稳定三级和四级蛋白质结构。在这里，我们研究了另一种涉及半胱氨酸的巯基的连接作用，即半胱氨酸和赖氨酸残基之间的分子内和分子间的亚甲基桥。在蛋白质数据库中确定了一些具有这种连接的晶体结构。对电子密度图的检查和对提名结构的重新精炼明确地证实了在几种情况下存在Lys-CH2-Cys键。
Cysteine residues ubiquitously stabilize tertiary and quaternary protein structure by formation of disulfide bridges. Here we investigate another linking interaction that involves sulfhydryl groups of cysteines, namely intra‐ and intermolecular methylene‐bridges between cysteine and lysine residues. A number of crystal structures possessing such a linkage were identified in the Protein Data Bank. Inspection of the electron density maps and re‐refinement of the nominated structures unequivocally confirmed the presence of Lys‐CH2‐Cys bonds in several cases.