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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
- Mechanism of regulation of proteinkisases CaMKK1, CaMKK2 and ASK1
- Study of inhibition of protease caspase-2 by 14-3-3 protein
- Study of DNA-binding domain of transcription factor FOXO4
- Interaction of cytoplasmatic domains of TRP channels
Projects
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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 two positively charged residues as having a crucial impact on PIP2/PIP3 binding.
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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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Achievements
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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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Publications
Jirků, Michaela - Bumba, Ladislav - Bednárová, Lucie - Kubala, M. - Šulc, Miroslav - Franěk, M. - Vyklický ml., Ladislav - Vondrášek, Jiří - Teisinger, Jan - Boušová, Kristýna
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Characterization of the part of N-terminal PIP2 binding site of the TRPM1 channel
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Biophysical Chemistry. 2015, Vol. 207, Dec, p. 135-142
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IF = 2.363
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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 = 4.258
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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 = 2.363
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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 = 4.348
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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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Crystal structure of RGS domain of G-protein signalization regulator RGS3 (PDB ID: 3L2C).
Molecular-dynamic simulation of a model of human melatonin MT2 receptor in a hydrated lipid bilayer. Mazna et al. (2008) J. of Pineal. Res.
