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

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: NMR analyses of the receiver domain of CKI1 histidine kinase and its interaction with AHP proteins Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	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. 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. (en)
Title	NMR analyses of the receiver domain of CKI1 histidine kinase and its interaction with AHP proteins NMR analyses of the receiver domain of CKI1 histidine kinase and its interaction with AHP proteins (en)
skos:prefLabel	NMR analyses of the receiver domain of CKI1 histidine kinase and its interaction with AHP proteins NMR analyses of the receiver domain of CKI1 histidine kinase and its interaction with AHP proteins (en)
skos:notation	RIV/00216224:14310/09:00039607!RIV10-MSM-14310___
http://linked.open...avai/riv/aktivita	P S Z
http://linked.open...avai/riv/aktivity	P(LC06030), P(LC06034), S, Z(MSM0021622413), Z(MSM0021622415)
http://linked.open...vai/riv/dodaniDat	2010
http://linked.open...aciTvurceVysledku	Hejátko, Jan Janda, Lubomír Dopitová, Radka Žídek, Lukáš Horák, Jakub Marek, Jaromír Pekárová, Blanka Třísková, Olga
http://linked.open.../riv/druhVysledku	O - Ostatní výsledky nezařaditelné do žádného z výše uvedených druhů výsledku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Masarykova univerzita / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	329609
http://linked.open...ai/riv/idVysledku	RIV/00216224:14310/09:00039607
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Histidine Kinase; CKI1; receiver domain; AHP proteins (en)
http://linked.open.../riv/klicoveSlovo	CKI1 receiver domain AHP proteins Histidine Kinase
http://linked.open...ontrolniKodProRIV	[B031A5F360C9]
http://linked.open...in/vavai/riv/obor	EB
http://linked.open...ichTvurcuVysledku	8 (xsd:int)
http://linked.open...cetTvurcuVysledku	8 (xsd:int)
http://linked.open...vavai/riv/projekt	Biomolecular centre Regulation of morphogenesis of plant cells and organs
http://linked.open...UplatneniVysledku	2009
http://linked.open...iv/tvurceVysledku	Dopitová, Radka Hejátko, Jan Horák, Jakub Janda, Lubomír Marek, Jaromír Žídek, Lukáš Pekárová, Blanka Třísková, Olga
http://linked.open...n/vavai/riv/zamer	Proteiny v metabolismu a při interakci organismů s prostředím Molecular basis of cell and tissue regulations
http://localhost/t...ganizacniJednotka	14310

Faceted Search & Find service v1.16.118 as of Jun 21 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 77 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software