The N-Terminal Domain of the Tomato Immune Protein Prf Contains Multiple Homotypic and Pto Kinase Interaction Sites
Date
2015
Authors
Saur, Isabel
Conlan, Brendon
Rathjen, John
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American Society for Biochemistry and Molecular Biology Inc
Abstract
Background: Plant immune proteins display complex conformations. Results: The Prf N-terminal domain forms a homo-dimer, has two binding sites for Pto kinase, and interacts with the Prf leucine-rich repeats domain. Conclusion: The Prf N-terminal domain coordinates multiple domain interactions to control the activity of the immune complex. Significance: Additional resolution is supplied to the Prf-Pto complex.
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Journal of Biological Chemistry
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Journal article
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Open Access
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