Source was cell extract of S2 cell line; protein derived from endogenous gene.
olf186-F is present primarily as homodimers in resting S2 cells.
Source was cell extract of S2 cell line; protein derived from endogenous gene.
olf186-F is present primarily as homodimers in resting S2 cells.
olf186-F subunits assemble into a hexameric calcium channel.
Interaction in vitro; protein produced as a recombinant fusion protein in bacterial system.
Crystal structure of H206A mutant form of olf186-F in open conformation. Hexameric.
Interaction in vitro; protein produced as recombinant fusion protein in a yeast system.
Interaction in vitro; protein produced as a recombinant fusion protein in baculoviral system.
The fragment of olf186-F used contains C224S, C283T mutations to increase protein stability and the channel activating mutation P288L. Structure is hexameric.
Interaction in vitro; protein produced as a recombinant fusion protein in baculoviral system.
The fragment of olf186-F used contains C224S, C283T mutations to increase protein stability and the channel activating mutation P288L. Structure is hexameric.
