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@proceedings{877331,
author = {Pekárová, Blanka and Třísková, Olga and Žídek, Lukáš and Marek, Jaromír and Horák, Jakub and Dopitová, Radka and Hejátko, Jan and Janda, Lubomír},
booktitle = {ACPD 2009 : Auxins and Cytokinins in Plant Development International Symposium},
keywords = {Histidine Kinase; CKI1; receiver domain; AHP proteins},
language = {eng},
title = {NMR analyses of the receiver domain of CKI1 histidine kinase and its interaction with AHP proteins},
url = {http://acpd.cas.cz/wp-content/uploads/2009/06/ACPD2009_Book_of_Abstracts.pdf},
year = {2009}
}
TY - CONF
ID - 877331
AU - Pekárová, Blanka - Třísková, Olga - Žídek, Lukáš - Marek, Jaromír - Horák, Jakub - Dopitová, Radka - Hejátko, Jan - Janda, Lubomír
PY - 2009
TI - NMR analyses of the receiver domain of CKI1 histidine kinase and its interaction with AHP proteins
KW - Histidine Kinase
KW - CKI1
KW - receiver domain
KW - AHP proteins
UR - http://acpd.cas.cz/wp-content/uploads/2009/06/ACPD2009_Book_of_Abstracts.pdf
N2 - In a multistep phosphorelay, the C-terminal receiver domain of sensor histidine kinases is supposed to be involved in protein-protein interactions with its downstream signalling partners, the AHP proteins. Here we show that CKI1RD interacts in vivo and in vitro with AHP2, 3, and 5 with different affinities. To understand protein-protein interactions on the molecular level, the structure of CKI1RD in solution has been studied in details by nuclear magnetic resonance (NMR). Effects of magnesium ions (Mg2+) and phosphate analogue beryllium fluoride on chemical shift changes of CKI1RD have been studied in a series of titration experiments and the most significantly affected residues were identified. Observed chemical shift changes were mapped on a solved crystallographic structure of the protein. Molecular motions were investigated by NMR relaxation experiments with free, Mg2+-bound, and beryllofluorinated CKI1RD. Based on these data and in combination with bioinformatics approach, we determined four regions that might be responsible for the observed specificity of protein-protein interactions between CKI1RD and individual AHP proteins.
ER -
PEKÁROVÁ, Blanka, Olga TŘÍSKOVÁ, Lukáš ŽÍDEK, Jaromír MAREK, Jakub HORÁK, Radka DOPITOVÁ, Jan HEJÁTKO a Lubomír JANDA. NMR analyses of the receiver domain of CKI1 histidine kinase and its interaction with AHP proteins. In \textit{ACPD 2009 : Auxins and Cytokinins in Plant Development International Symposium}. 2009.
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