The N-Terminal Domain of the Tomato Immune Protein Prf Contains Multiple Homotypic and Pto Kinase Interaction Sites
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Saur, Isabel; Conlan, Brendon; Rathjen, John
Description
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 |
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Date published: | 2015 |
Type: | Journal article |
URI: | http://hdl.handle.net/1885/70026 |
Source: | Journal of Biological Chemistry |
DOI: | 10.1074/jbc.M114.616532 |
Access Rights: | Open Access |
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01_Saur_The_N-Terminal_Domain_of_the_2015.pdf | 2.73 MB | Adobe PDF |
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