The world of GPCR dimers - mapping dopamine receptor D2 homodimers in different activation states and configuration arrangements

<p>G protein-coupled receptors (GPCRs) are known to dimerize, but the molecular and structural basis of GPCR dimers is not well understood. We developed a computational framework to generate models of the&nbsp;dopamine receptor D2 (D₂R) homodimer in different activation states of the monomers and identified their most likely interfaces with molecular detail and contacts formed between interfacial residues. Such contacts were followed along a 3 replicates of 500 ns molecular dynamics simulation.&nbsp;</p> <p>The dataset presented here is a summary of all interfacial contacts, such as hydrogen bonds, pi-cation, pi-stacking, salt-bridges and t-stacking interactions, which occur within the interfaces of the different dimer configurations. The information can be viewed as dynamical flareplots, by uploading the .json files to&nbsp;https://gpcrviz.github.io/flareplot/.&nbsp;</p> <p>Contacts were measured using GetContacts (https://getcontacts.github.io/).</p> <p>&nbsp;</p> <p>6CM4-6CM4 = inactive-inactive</p> <p>6CM4-6U1N = inactive-arrestin</p> <p>6U1N-6U1N = arrestin-arrestin</p> <p>6VMS-6CM4 = active-inactive</p> <p>6VMS-6U1N = active-arrestin</p> <p>6VMS-6VMS = active-active</p>