Publication | Closed Access
Visualizing Tyrosine Kinase Activity with Bipartite Tetracysteine Display
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Citations
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References
2010
Year
Bias BindingMolecular BiologyLinear Tetracysteine SequenceProtein FoldingReceptor Tyrosine KinaseCell SignalingTyrosine Kinase ActivityProtein FunctionBiochemistryBiochemical InteractionProtein ModelingBiomolecular InteractionSrc-family Kinase SensorProtein BioinformaticsBiomolecular ScienceProtein PhosphorylationSignal TransductionNatural SciencesCellular BiochemistrySystems BiologyMedicineSmall MoleculesDrug Discovery
BiAs binding: Recently we reported that the linear tetracysteine sequence preferred by FlAsH and ReAsH could be split between two members of a protein partnership or regions of a folded protein, while maintaining high affinity and brightness. Here we show that this tool—bipartite tetracysteine display—facilitates the design of E2, an encodable, site-selective, Src-family kinase sensor. Detailed facts of importance to specialist readers are published as ”Supporting Information”. Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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