Structural analysis of ATP analogues compatible with kinase-catalyzed labeling.

Structural analysis of ATP analogues compatible with kinase-catalyzed labeling.
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与激酶催化标记兼容的 ATP 类似物的结构分析。

DOI:
10.1021/bc300404s
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发表时间:
2012
影响因子:
4.7
通讯作者:
Pflum,MaryKayH
Pflum,MaryKayH
中科院分区:
化学2区
文献类型:
--
作者:
Suwal,Sujit;Senevirathne,Chamara;Garre,Satish;Pflum,MaryKayH

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Kinase-catalyzed protein phosphorylation is an important biochemical process involved in cellular functions. We recently discovered that kinases promiscuously accept γ-modified ATP analogues as cosubstrates and used several ATP analogues as tools for studying protein phosphorylation. Herein, we explore the structural requirements of γ-modified ATP analogues for kinase compatibility. To understand the influence of linker length and composition, a series of ATP analogues was synthesized, and the efficiency of kinase-catalyzed labeling was determined by quantitative mass spectrometry. This study on factors influencing kinase cosubstrate promiscuity will enable design of ATP analogues for a variety of kinase-catalyzed labeling reactions.
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