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

dc.contributor.authorSaur, Isabel
dc.contributor.authorConlan, Brendon
dc.contributor.authorRathjen, John
dc.date.accessioned2015-12-10T23:36:10Z
dc.date.issued2015
dc.date.updated2015-12-10T11:51:50Z
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.identifier.issn0021-9258
dc.identifier.urihttp://hdl.handle.net/1885/70026
dc.publisherAmerican Society for Biochemistry and Molecular Biology Inc
dc.rightsAuthor/s retain copyrighten_AU
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
dcterms.accessRightsOpen Accessen_AU
local.bibliographicCitation.issue18
local.bibliographicCitation.lastpage11267
local.bibliographicCitation.startpage11258
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.contributor.authoruidSaur, Isabel, u1820430
local.contributor.authoruidConlan, Brendon, u4175143
local.contributor.authoruidRathjen, John, u3753288
local.description.notesImported from ARIES
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.absseo970106 - Expanding Knowledge in the Biological Sciences
local.identifier.ariespublicationa383154xPUB2199
local.identifier.citationvolume290
local.identifier.doi10.1074/jbc.M114.616532
local.identifier.scopusID2-s2.0-84929500822
local.type.statusPublished Version

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