NMR analyses of the receiver domain of CKI1 histidine kinase and its interaction with AHP proteins

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F09%3A00039607" target="_blank" >RIV/00216224:14310/09:00039607 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

NMR analyses of the receiver domain of CKI1 histidine kinase and its interaction with AHP proteins

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

NMR analyses of the receiver domain of CKI1 histidine kinase and its interaction with AHP proteins

Popis výsledku anglicky

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.

Druh

O - Ostatní výsledky

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2009

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů