Detailed Information on Publication Record
2010
Dynamic structure and binding specifity of the receiver domain of sensor histidine kinase CKI1
PEKÁROVÁ, Blanka, Tomáš KLUMPLER, Olga TŘÍSKOVÁ, Jakub HORÁK, Lukáš ŽÍDEK et. al.Basic information
Original name
Dynamic structure and binding specifity of the receiver domain of sensor histidine kinase CKI1
Name in Czech
Dynamika struktury a vazebná specifita přijímačové domény senzorové histidinkinázy CKI1
Authors
PEKÁROVÁ, Blanka, Tomáš KLUMPLER, Olga TŘÍSKOVÁ, Jakub HORÁK, Lukáš ŽÍDEK, Jaromír MAREK, Radka DOPITOVÁ, Jan HEJÁTKO and Lubomír JANDA
Edition
Tarragona, Spain, p. 85-86, 2 pp. 2010
Publisher
IPGSA conference 2010
Other information
Language
English
Type of outcome
Stať ve sborníku
Field of Study
10600 1.6 Biological sciences
Country of publisher
Spain
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Organization unit
Faculty of Science
Keywords in English
multistep phosphorelay, crystal structure, NMR analysis, CKI1
Změněno: 29/4/2011 15:32, RNDr. Lubomír Janda, Ph.D.
Abstract
V originále
In the Arabidopsis two-component signaling, the signal is transfered from sensor histidine kinase via histidine-containing phosphotransfer proteins (AHP1-5) to nuclear response regulators. Here we show the receiver domain of histidine kinase CYTOKININ-INDEPENDENT1 (CKI1RD) interacts in vivo and in vitro with AHP2, 3 and 5 with different affinities. To unravel the molecular determinants of observed specificity, we determined crystal structure of free CKI1RD and CKI1RD in complex with magnesium ions. Dynamics of CKI1RD solution structure has been studied in details by NMR in absence or presence of magnesium ions and beryllium fluoride.
Links
GA521/09/1699, research and development project |
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LC06034, research and development project |
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MSM0021622413, plan (intention) |
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MSM0021622415, plan (intention) |
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