Intranet Čeština

Protein Structures

Protein Structures

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
  • 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

PIP2 and PIP3 interact with N-terminus region of TRPM4 channel

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.  More

Achievements

Tomáš Obšil was awarded the title of professor

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. More

Publications

Jirků, Michaela - Bumba, Ladislav - Bednárová, Lucie - Kubala, M. - Šulc, Miroslav - Franěk, M. - Vyklický ml., Ladislav - Vondrášek, Jiří - Teisinger, Jan - Boušová, Kristýna . Characterization of the part of N-terminal PIP2 binding site of the TRPM1 channel . Biophysical Chemistry. 2015, Vol. 207, Dec, p. 135-142 . IF = 2.363 [ASEP] [ doi ]
Kacířová, Miroslava - Košek, Dalibor - Kádek, Alan - Man, Petr - Večeř, J. - Herman, P. - Obšilová, Veronika - Obšil, Tomáš . Structural Characterization of Phosducin and Its Complex with the 14-3-3 Protein . Journal of Biological Chemistry. 2015, Vol. 290, 26, p. 16246-16260 . IF = 4.258 [ASEP] [ doi ]
Boušová, Kristýna - Jirků, Michaela - Bumba, Ladislav - Bednárová, Lucie - Šulc, Miroslav - Franěk, M. - Vyklický ml., Ladislav - Vondrášek, Jiří - Teisinger, Jan . PIP2 and PIP3 interact with N-terminus region of TRPM4 channel . Biophysical Chemistry. 2015, Vol. 205, Oct 2015, p. 24-32 . IF = 2.363 [ASEP] [ doi ]
Gryčová, Lenka - Holendová, Blanka - Lánský, Zdeněk - Bumba, Ladislav - Jirků, Michaela - Boušová, Kristýna - Teisinger, Jan . Ca2+ Binding Protein S100A1 Competes with Calmodulin and PIP2 for Binding Site on the C-Terminus of the TPRV1 Receptor . ACS Chemical Neuroscience. 2015, Vol. 6, 3, p. 386-392 . IF = 4.348 [ASEP] [ doi ]
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 . Physiological Research 2014, roč. 63, suppl.1, s155-s164. ISSN 0862-8408. IF = 1.293 [ASEP]

Article photogallery

The entire photogallery

Contacts

Institute of Physiology AS CR, v.v.i.
Department of Protein Structures

Vídeňská 1083
14220 Prague 4
tel. +420 241 062 191
fax. +420 241 062 477
 

veronika.obsilova@fgu.cas.cz

People

RNDr. Veronika Obšilová, Ph.D.
head of the department
Prof. RNDr. Tomáš Obšil, Ph.D.
deputy head of department

RNDr. Miroslava Alblová (born Kopecká), Ph.D.
junior researcher

Ing. Jan Teisinger, CSc.
senior researcher
Ing. Michaela Jirků
PhD student
Mgr. Kristýna Boušová
PhD student
Mgr. Salome Kylarová
PhD student
Mgr. Dana Kalábová (born Žáková) 
PhD student
Bc. Aneta Šmídová
PhD student

Mgr. Olívia Petrvalská
PhD student

Mgr. Katarína Pšenáková
PhD student
   
Bc. Kateřina Jarosilová
undergraduate student
Simona Krausová
lab technician

© 2014 INSTITUTE OF PHYSIOLOGY CAS