TY - JOUR
T1 - The N-terminal domain of the tomato immune protein prf contains multiple homotypic and pto kinase interaction sites
AU - Saur, Isabel Marie Luise
AU - Conlan, Brendon Francis
AU - Rathjen, John Paul
N1 - Publisher Copyright:
© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.
PY - 2015/5/1
Y1 - 2015/5/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84929500822&partnerID=8YFLogxK
U2 - 10.1074/jbc.M114.616532
DO - 10.1074/jbc.M114.616532
M3 - Article
SN - 0021-9258
VL - 290
SP - 11258
EP - 11267
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 18
ER -