http://www.biomed.cas.cz/d312/index.php?section=home
Our group is focused on structural biology (the relationship between the structure and function of certain groups of proteins), particularly we focus on the proteins which participate in the signal transmission in the cell. Among methods we use are recombinant protein expression, biophysical characterization, study of intermolecular interactions, protein structure and interaction surfaces. All these methods enable us to better understand the details how the activity and function of protein-protein complexes is regulated. Our research is focused mainly on:
- Structural biology of 14-3-3 proteins and their complexes
- Study of DNA-binding domain of transcription factor FOXO4
- Mechanism of regulation of Ask kinases
- Interaction of cytoplasmatic domains of TRP channels
Projects
Our results show the activation of yeast neutral trehalase Nth1 by 14-3-3 proteins from the structural point of view. Our data could be important for understanding of the activation process of Nth1 as well as of the role of 14-3-3 proteins in the regulation of other enzymes.
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Phosducin (Pdc), a highly conserved phosphoprotein, plays an important role in the regulation of G-protein signalling, transcriptional control, and modulation of blood pressure. Pdc is negatively regulated by phosphorylation followed by binding to the 14-3-3 protein.
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Transient receptor potential (TRP) channels are a wide family of non-selective ion channels responsible for monovalent and divalent cation influx into the cells. Members of this family are involved in many sensory processes. We identified several positively charged residues as having a crucial impact on CaM/S100A1 binding.
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Achievements
Kacirova M, Kosek D, Kadek A, Man P, Vecer J, Herman P, Obsilova V and Obsil T
J. Biol. Chem. jbc.M115.636563. First Published on May 13, 2015, doi:10.1074/jbc.M115.636563
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Prof. RNDr. Tomáš Obšil, Ph.D. was awarded by the title of professor at The Faculty of Science, Charles University, majoring in Physical Chemistry. Professors graduation will take place December 18, 2014.
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Kopecka M, Kosek D, Kukacka Z, Rezabkova L, Man P, Novak P, Obsil T, Obsilova V.
J Biol Chem. 2014 May 16;289(20):13948-61.
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Kosek D, Kylarova S, Psenakova K, Rezabkova L, Herman P, Vecer J, Obsilova V, Obsil T.
J Biol Chem. 2014 Aug 29;289(35):24463-74.
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Publications
Kacířová, Miroslava - Košek, Dalibor - Kádek, Alan - Man, Petr - Večeř, J. - Herman, P. - Obšilová, Veronika - Obšil, Tomáš
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Structural Characterization of Phosducin and Its Complex with the 14-3-3 Protein
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Journal of Biological Chemistry. 2015, Vol. 290, 26, p. 16246-16260
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IF = 4.573
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Gryčová, Lenka - Holendová, Blanka - Lánský, Zdeněk - Bumba, Ladislav - Jirků, Michaela - Boušová, Kristýna - Teisinger, Jan
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Ca2+ Binding Protein S100A1 Competes with Calmodulin and PIP2 for Binding Site on the C-Terminus of the TPRV1 Receptor
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ACS Chemical Neuroscience. 2015, Vol. 6, 3, p. 386-392
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IF = 4.362
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Boušová, Kristýna - Jirků, Michaela - Bumba, Ladislav - Bednárová, Lucie - Šulc, Miroslav - Franěk, M. - Vyklický ml., Ladislav - Vondrášek, Jiří - Teisinger, Jan
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PIP2 and PIP3 interact with N-terminus region of TRPM4 channel
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Biophysical Chemistry. 2015, Vol. 205, Oct 2015, p. 24-32
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IF = 1.986
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Obšilová, Veronika - Kopecká, Miroslava - Košek, Dalibor - Kacířová, M. - Kylarová, Salome - Řežábková, L. - Obšil, T.
Mechanisms of the 14-3-3 protein function: regulation of protein function through conformational modulation
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Physiological Research 2014, roč. 63, suppl.1, s155-s164. ISSN 0862-8408.
IF = 1.293
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Košek, Dalibor - Kylarová, Salome - Pšenáková, Katarína - Řežábková, L. - Herman, P. - Večeř, J. - Obšilová, Veronika - Obšil, T.
Biophysical and Structural Characterization of the Thioredoxin-binding Domain of Protein Kinase ASK1 and Its Interaction with Reduced Thioredoxin
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Journal of Biological Chemistry 2014, roč. 289, 35, p. 24463-24474. ISSN 0021-9258.
IF = 4.573
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Model of a possible conformational change of C-tail segment of 14-3-3ζ protein due to phosphorylation of T232. Obsilova et al. (2004) JBC
Crystal structure of DNA-binding domain of forkhead transcription factor FOXO4 bound to the DNA (PDB ID: 3L2C).
