Structures of proteins and their complexes modeled by BIOmodeling group available for downloading.

Publications Models Figures
S. Yuan, U. Ghoshdastider, B. Trzaskowski, D. Latek, A. Debinski, W. Pulawski, R. Wu, V. Gerke, S. Filipek, The role of water in activation mechanism of human N formyl Peptide Receptor 1 (FPR1) based on molecular dynamics simulations, PLOS ONE (2012) 7, e47114. doi: 10.1371/journal.pone.0047114. Formyl Peptide Receptor 1 (FPR1) with agonist fMLF with antagonist tBocMLF. The models contain water molecules within a distance < 3 Å from the complex. Agonist fMLF located deep in binding site of FPR1.
T.M. Stepniewski, S. Filipek, Non-peptide ligand binding to the formyl peptide receptor FPR2 - a comparison to peptide ligand binding modes, Bioorg. Med. Chem. (2015) 23, 4072-4081. doi: 10.1016/j.bmc.2015.03.062. Model of free FPR2 and a complex of FPR2 with agonist fMLFK. Zones in the orthosteric binding site of FPR2.

  • April 2019.
    Our latest review on "Molecular switches in GPCRs".

  • March 2019.
    The ERNEST project (COST CA18133) has started.
    ERNEST = European Research Network on Signal Transduction
    The main scientific objective of the Action is to develop a common, comprehensive and holistic map of signal transduction that will advance development of pathway-specific chemical modulators. This unique and innovative goal will be realised by linking of a diverse group of researchers in the field through the networking activities funded by COST.
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