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.||Model of free FPR2 and a complex of FPR2 with agonist fMLFK.||Zones in the orthosteric binding site of FPR2.|
THE LATEST NEWS
- August 2022.COGRIMEN
- June 2021.GPCRsignalOur new service GPCRsignal was recently published in NAR 2021, W1.
- 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 TransductionThe 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.