Hortin G, Folz R, Gordon J I, Strauss A W
Biochem Biophys Res Commun. 1986 Nov 26;141(1):326-33. doi: 10.1016/s0006-291x(86)80372-2.
A wide variety of secretory proteins have recently been found to undergo post-translational sulfation of specific tyrosine residues. Here, amino acid sequences surrounding known sulfation sites in proteins are analyzed in order to identify factors which determine the specificity of sulfation. Several distinctive features of sulfation sites are identified, including: abundance of acidic amino acid residues, lack of basic residues, low hydropathy, absence of neighboring cysteine residues, lack of extended secondary structure. Rules are proposed for predicting likely sites of sulfation based on the amino acid sequence of a protein.
最近发现多种分泌蛋白会发生特定酪氨酸残基的翻译后硫酸化修饰。在此,对蛋白质中已知硫酸化位点周围的氨基酸序列进行分析,以确定决定硫酸化特异性的因素。确定了硫酸化位点的几个显著特征,包括:酸性氨基酸残基丰富、缺乏碱性残基、亲水性低、不存在相邻的半胱氨酸残基、缺乏延伸的二级结构。基于蛋白质的氨基酸序列,提出了预测可能硫酸化位点的规则。