Fig. 5

ORP1-ORD has three oligomeric states in vitro and in vivo. a Gel filtration analyses of ORP1S in isolation and in complex with cholesterol. b Immunoblot analysis of the oligomeric states of ORP1S. c, d The domain-swapping dimer (c) and trimer (d) of cholesterol-bound ORP1-ORD. e Close-up view of the domain-swapping interactions between the N-terminal loop (blue) and the symmetry-related core (orange) in the dimer shown in c. f Snapshots at indicated time points during the MD simulations for monomeric ORP1-ORD complexed with cholesterol