Crystal structure of CKI1 receiver domain from Arabidopsis
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F09%3A00039825" target="_blank" >RIV/00216224:14310/09:00039825 - isvavai.cz</a>
Result on the web
—
DOI - Digital Object Identifier
—
Alternative languages
Result language
angličtina
Original language name
Crystal structure of CKI1 receiver domain from Arabidopsis
Original language description
Sensor histidine kinases (HKs) are members of the two-component (TC) signalling systems that mediate signal transduction in a broad spectrum of adaptive responses in bacteria. The sensor histidine kinase CKI1 was identified as an activator of a cytokinin-like response when overexpressed in hypocotyl explants of A. thaliana. However, in contrast to the genuine cytokinin receptors of A. thaliana, AHK2, AHK3 and AHK4, CKI1 was found to be constitutively active in bacteria and yeast or A. thaliana protoplasts. Thus, the specificity and the role of CKI1 in the TC signalling in A. thaliana remain unclear. The three-dimensional structure of A. thaliana CKI1RD was determined. The catalytic aspartate residue is located on the carboxyl terminus of the central beta3-strand, in a cavity formed by loops L1, L5 and L7 loops. All major conformational differences between receiver proteins are located in the loops, which supposedly form a docking interface for the ineracting partners.
Czech name
—
Czech description
—
Classification
Type
O - Miscellaneous
CEP classification
EB - Genetics and molecular biology
OECD FORD branch
—
Result continuities
Project
<a href="/en/project/LC06034" target="_blank" >LC06034: Regulation of morphogenesis of plant cells and organs</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2009
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů