ArticleACS chemical biology2015
A selective NMR probe to monitor the conformational transition from inactive to active kinase.
Article in ACS chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- HKPocket: human kinase pocket database for drug design.BMC bioinformatics · 2019Article
- Cysteine-ethylation of tissue-extracted membrane proteins as a tool to detect conformational states by solid-state NMR spectroscopy.Methods in enzymology · 2019Article
- ProteinJournal of biomolecular NMR · 2017Article
- Ca(2+) ATPase Conformational Transitions in Lipid Bilayers Mapped by Site-directed Ethylation and Solid-State NMR.ACS chemical biology · 2016Article
- Evaluation of colorimetric assays for analyzing reductively methylated proteins: Biases and mechanistic insights.Analytical biochemistry · 2015Article
- 13C NMR detects conformational change in the 100-kD membrane transporter ClC-ec1.Journal of biomolecular NMR · 2015Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Kinases control many aspects of cellular signaling and are therefore therapeutic targets for numerous disease states. Monitoring the conformational changes that drive activation and inactivation of the catalytic kinase core is a challenging experimental problem due to the dynamic nature of these enzymes. We apply [(13)C] reductive methylation to chemically introduce NMR-active nuclei into unlabeled protein kinases. The results demonstrate that solution NMR spectroscopy can be used to monitor specific changes in the chemical environment of structurally important lysines in a [(13)C]-methylated kinase as it shifts from the inactive to active state. This approach provides a solution based method to complement X-ray crystallographic data and can be applied to nearly any kinase, regardless of size or method of production.
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Registered trials
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