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