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

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 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. 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 https://gpcrviz.github.io/flareplot/. Contacts were measured using GetContacts (https://getcontacts.github.io/). 6CM4-6CM4 = inactive-inactive 6CM4-6U1N = inactive-arrestin 6U1N-6U1N = arrestin-arrestin 6VMS-6CM4 = active-inactive 6VMS-6U1N = active-arrestin 6VMS-6VMS = active-active