The N-Terminal Domain of the Tomato Immune Protein Prf Contains Multiple Homotypic and Pto Kinase Interaction Sites
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.
|Collections||ANU Research Publications|
|Source:||Journal of Biological Chemistry|
|01_Saur_The_N-Terminal_Domain_of_the_2015.pdf||2.73 MB||Adobe PDF|
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