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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 and 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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