Structures of proteins and their complexes modeled by BIOmodeling group available for downloading.
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.
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.
Our service GPCRM is completely reshaped, much faster, and user friendly. Now, it contains 3 main routes: Quick path (default), Long path, and High similarity (the fastest) for homology modeling of GPCRs. Currently, the service contains over 90 template structures. The updated version was recently published in NAR 2018, W1.