Role of amino acid residues surrounding the phosphorylation site in peptide substrates of G protein-coupled receptor kinase 2 (GRK2)
Role of amino acid residues surrounding the phosphorylation site in peptide substrates of G protein-coupled receptor kinase 2 (GRK2)
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DOI：
10.1007/s00726-016-2345-6
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发表时间：
2016-12-01
期刊：
影响因子：
3.5
通讯作者：
Kang, Jeong-Hun
中科院分区：
文献类型：
--
作者：
Asai, Daisuke;Murata, Masaharu;Kang, Jeong-Hun
在先前鉴定的β-微管蛋白衍生的GRK 2底物肽（（404）DEMEFTEAESNMN（416））中进行一系列氨基酸取代，以检查磷酸化位点周围的氨基酸残基的作用。磷酸化位点周围的阴离子氨基酸残基在GRK 2的亲和力中起重要作用。与原始肽相比，修饰的肽（Ac-EEMEFSEAEANMN-NH 2）对GRK 2表现出明显更高的亲和力，但对GRK 5表现出非常低的亲和力，这表明它可以是GRK 2的敏感和选择性肽。
A series of amino acid substitutions was made in a previously identified beta-tubulin-derived GRK2 substrate peptide ((404)DEMEFTEAESNMN(416)) to examine the role of amino acid residues surrounding the phosphorylation site. Anionic amino acid residues surrounding the phosphorylation site played an important role in the affinity for GRK2. Compared to the original peptide, a modified peptide (Ac-EEMEFSEAEANMN-NH2) exhibited markedly higher affinity for GRK2, but very low affinity for GRK5, suggesting that it can be a sensitive and selective peptide for GRK2.