Abstract
Background: Kinetic modulations of Arf1-Sec7 domain complex, by the uncompetitive inhibitor brefeldin A and allosteric factors, are not established. Results: Brefeldin A reorients the binary Arf1-Sec7 domain complex to an abortive one with reduced association and dissociation rates. Conclusion: Kinetic hallmarks allow distinguishing the level, nature, and fate of interacting species. Significance: Similar approach will solve the inhibitory mechanism of new inhibitor families of sec7 domains.© 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Rouhana, J., Padilla, A., Estaran, S., Bakari, S., Delbecq, S., Boublik, Y., … Chavanieu, A. (2013). Kinetics of interaction between ADP-ribosylation factor-1 (Arf1) and the Sec7 domain of arno guanine nucleotide exchange factor, modulation by allosteric factors, and the uncompetitive inhibitor brefeldin A. Journal of Biological Chemistry, 288(7), 4659–4672. https://doi.org/10.1074/jbc.M112.391748
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