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The N-Terminal Domain of the Tomato Immune Protein Prf Contains Multiple Homotypic and Pto Kinase Interaction Sites

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Date

2015

Authors

Saur, Isabel
Conlan, Brendon
Rathjen, John

Journal Title

Journal ISSN

Volume Title

Publisher

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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Keywords

Citation

URI

http://hdl.handle.net/1885/70026

Collections

ANU Research Publications

Source

Journal of Biological Chemistry

Type

Journal article

Book Title

Entity type

Access Statement

Open Access

License Rights

DOI

10.1074/jbc.M114.616532

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