We are not only Users but we actively contribute to scientific software. We developed two web applications for modeling of G protein-coupled receptors: GUT-DOCK & GPCRM and one standalone program for using sparse NMR data in protein structure prediction - CABS-NMR and contributed to INPHARMA.
Our recent project is focused on: Resources for GPCR research.
Scripts for processing of MD trajectories.
"Structural studies based on the low sequence similarity of G-protein coupled receptors activated by hormones and allosteric modulators.", National Science Centre in Poland, grant no DEC-2012/07/D/NZ1/04244
Post-doc in the Laboratory of Prof. Filipek in the International Institute of Molecular and Cell Biology in Warsaw. Short-term post-doc fellowships: EMBL-Heidelberg, University of California San Francisco.
PhD studies in the Laboratory of Prof. Kolinski, Faculty of Chemistry, University of Warsaw. PhD thesis title: "Protein structure determination using sparse experimental data", MNiSW grant for PhD students: „Modeling of protein structures based on fragmentary data from simple NMR experiments”.
'Identifying new GPCR drugs will need additional detailed knowledge of GPCR biology, especially knowledge from structural biology, given the complex structure–function relationships involved in GPCR signaling. [...] In this respect, nuclear magnetic resonance (NMR) spectroscopy in solution is a key tool for analysing function-related conformational equilibria in GPCRs as they relate to allosteric coupling, variable efficacies and biased signaling of GPCR ligands... '
'GPR158, a class C orphan GPCR, functions in cognition, stress-induced mood control, and synaptic development. Among class C GPCRs, GPR158 is unique as it lacks a Venus flytrap-fold ligand-binding domain and terminates Galphai/o protein signaling through the RGS7-Gbeta5 heterodimer. Here, we report the cryo-EM structures of GPR158 alone and in complex with one or two RGS7-Gbeta5 heterodimers.'
'G-protein-coupled receptors (GPCRs) are divided phylogenetically into six classes, denoted A to F. More than 370 structures of vertebrate GPCRs (belonging to classes A, B, C and F) have been determined [...]. Here we determine the structure of a [first] class D GPCR, the Saccharomyces cerevisiae pheromone receptor Ste2, in an active state coupled to the heterotrimeric G protein Gpa1–Ste4–Ste18. Ste2 was purified as a homodimer coupled to two G proteins.'
'Rational structure-based drug design (SBDD) relies on the availability of a large number of co-crystal structures to map the ligand-binding pocket of the target protein and use this information for lead-compound optimization via an iterative process.[...] Here, a method is presented for the rapid determination of multiple co-crystal structures for a target GPCR in complex with various ligands, taking advantage of the serial femtosecond crystallography approach, which obviates the need for large crystals and requires only submilligram quantities of purified protein.'
'Classically, G-protein-coupled receptors (GPCRs) are thought to activate G protein from the plasma membrane and are subsequently desensitized by Beta-arrestin (Beta-arr). However, some GPCRs continue to signal through G protein from internalized compartments, mediated by a GPCR–G protein–Beta-arr ‘megaplex’. [...] Here, we present its cryo-electron microscopy structure'
'The world’s first superconducting megahertz repetition rate hard X-ray free-electron laser (XFEL), the European XFEL, began operation in 2017, featuring a unique pulse train structure with 886 ns between pulses. [...] Here, we report the first membrane protein megahertz SFX experiment, where we determined a 2.9 Å-resolution SFX structure of the large membrane protein complex, Photosystem I, a > 1 MDa complex containing 36 protein subunits and 381 cofactors.'
dlatek at chem.uw.edu.pl
Faculty of Chemistry UW
1 Pasteur St., 02-093 Warsaw