Recognition of proximally phosphorylated tyrosine residues and continuous analysis of phosphatase activity using a stable europium complex
Recognition of proximally phosphorylated tyrosine residues and continuous analysis of phosphatase activity using a stable europium complex
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DOI：
10.1080/10610278.2017.1410548
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发表时间：
2018-01-01
影响因子：
3.3
通讯作者：
Butler, Stephen J.
中科院分区：
文献类型：
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作者：
Hewitt, Sarah H.;Liu, Roanna;Butler, Stephen J.
使用合成分子识别蛋白质及其翻译后修饰是一个活跃的研究领域。常见的翻译后修饰是丝氨酸、苏氨酸或酪氨酸残基的磷酸化。近端酪氨酸残基的磷酸化发生在人类蛋白质组中超过1000种蛋白质中，包括疾病相关蛋白质，因此对该基序的识别特别感兴趣。我们已经开发了一种发光铕（III）配合物，[Eu.1]（+），能够区分近端磷酸化的酪氨酸残基，从类似的单和非磷酸化的酪氨酸残基，更远相关的磷酸酪氨酸残基和近端磷酸化的丝氨酸和苏氨酸残基。[Eu.1]（+）用于连续监测磷酸酶催化的含有近端磷酸化酪氨酸残基的肽的去磷酸化。
The recognition of proteins and their post-translational modifications using synthetic molecules is an active area of research. A common post-translational modification is the phosphorylation of serine, threonine or tyrosine residues. The phosphorylation of proximal tyrosine residues occurs in over 1000 proteins in the human proteome, including in disease-related proteins, so the recognition of this motif is of particular interest. We have developed a luminescent europium(III) complex, [Eu.1](+), capable of the discrimination of proximally phosphorylated tyrosine residues, from analogous mono- and non-phosphorylated tyrosine residues, more distantly-related phosphotyrosine residues and over proximally phosphorylated serine and threonine residues. [Eu.1](+) was used to continuously monitor the phosphatase catalysed dephosphorylation of a peptide containing proximally phosphorylated tyrosine residues.