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

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.

Description

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Citation

Source

Journal of Biological Chemistry

Type

Journal article

Book Title

Entity type

Access Statement

Open Access

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