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National Repository of Grey Literature 12 records found  previous11 - 12  jump to record: Search took 0.00 seconds. 
Study of interactions between protein kinase CaMKK2 and calmodulin using fluorescence spectroscopy.
 Mikulů, Martina ; Obšil, Tomáš (advisor) ; Pavlíček, Jiří (referee)
Ca2+ /calmodulin-dependent kinases are members of CaMK family, which is involved in CaMK cascade. One of CaMK family members is Ca2+ /calmodulin-dependent kinase kinase 2 (CaMKK2), which is activated by Ca2+ /CaM-binding. There are some structural differences between CaMKK2 and other protein kinases, one of them is a structure near αE-helix and autoinhibitory domain. Due to the overlap of autoinhibitory domain and Ca2+ /CaM-binding domain it can be supposed that Ca2+ /CaM-binding induces structural changes near autoinhibitory do- main and thus can affect the accessibility of this region. CaMKK2 W445F mutant, which contains only one tryptophane residue Trp374 close to the αE-helix, was expressed and purified. Structural changes in this region were monitored using tryptophan fluorescence intensity quenching experiments, which can provide information about the accessibility of region surrounding tryptophan residue. The fluorescence of Trp374 was quenched using acrylamide. Comparison of fluorescence quenching experiments performed in the presence and absence of calmodulin suggests that the complex formation induces structural change in the region surrounding Trp374 . 1
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Preparation of thioredoxin and thioredoxin-binding domain of protein kinase ASK1 for structural studies
 Jarosilová, Kateřina ; Obšil, Tomáš (advisor) ; Kalábová, Dana (referee)
All living organisms are exposed to various forms of stress during their lifetime. This is probably the reason why an evolutionally well conserved the mitogen-activated protein kinase (MAPK) system of signaling cascades was formed to regulate cellular stress response. Those signaling pathways consist of three consecutive classes of protein kinases: MAP3K, MAP2K and MAPK. The signal is then transmitted from MAPK to another protein kinases and transcription factors. Apoptosis signal-regulating kinase 1 (ASK1) is a member of MAPK pathway, more specifically is classified as a member of the mitogen-activated protein kinase kinase kinase family (MAP3K). Human ASK1 consists of 1374 amino acids which are folded into several domains and sequence motives. The N-terminal coil-coiled domain (NCC), the serine/threonine kinase domain and the C-terminal coil-coiled domain (CCC) are three main domains. In addition, several regions responsible for the interaction between ASK1 and their binding partners have also been identified. The activity of ASK1 is regulated by various factors including thioredoxin and the 14-3-3 proteins, which function as inhibitors, and TNF receptor associated factors (TRAFs), which function as activators. The aim of this study was the preparation of six different expression constructs of...
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National Repository of Grey Literature : 12 records found   previous11 - 12  jump to record:
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