Skip navigation
Skip navigation

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

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.

dc.contributor.authorSaur, Isabel
dc.contributor.authorConlan, Brendon
dc.contributor.authorRathjen, John
dc.date.accessioned2015-12-10T23:36:10Z
dc.identifier.issn0021-9258
dc.identifier.urihttp://hdl.handle.net/1885/70026
dc.description.abstractBackground: 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.
dc.publisherAmerican Society for Biochemistry and Molecular Biology Inc
dc.rightsAuthor/s retain copyright
dc.sourceJournal of Biological Chemistry
dc.titleThe N-Terminal Domain of the Tomato Immune Protein Prf Contains Multiple Homotypic and Pto Kinase Interaction Sites
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume290
dc.date.issued2015
local.identifier.absfor060700 - PLANT BIOLOGY
local.identifier.absfor060703 - Plant Developmental and Reproductive Biology
local.identifier.absfor060199 - Biochemistry and Cell Biology not elsewhere classified
local.identifier.ariespublicationa383154xPUB2199
local.type.statusPublished Version
local.contributor.affiliationSaur, Isabel, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationConlan, Brendon, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationRathjen, John, College of Medicine, Biology and Environment, ANU
local.bibliographicCitation.issue18
local.bibliographicCitation.startpage11258
local.bibliographicCitation.lastpage11267
local.identifier.doi10.1074/jbc.M114.616532
local.identifier.absseo970106 - Expanding Knowledge in the Biological Sciences
dc.date.updated2015-12-10T11:51:50Z
local.identifier.scopusID2-s2.0-84929500822
dcterms.accessRightsOpen Access
CollectionsANU Research Publications

Download

File Description SizeFormat Image
01_Saur_The_N-Terminal_Domain_of_the_2015.pdf2.73 MBAdobe PDF


Items in Open Research are protected by copyright, with all rights reserved, unless otherwise indicated.

Updated:  19 May 2020/ Responsible Officer:  University Librarian/ Page Contact:  Library Systems & Web Coordinator