Abstract:
:The secondary structures of and the interactions between the intracellular domains (the three loops and the C-terminal tail) of the mouse-derived prostaglandin E2 receptor EP3beta subtype were investigated using peptides mimicking the domains. The N-termini of the peptides were palmitoylated to anchor on unilamellar vesicles composed of phosphatidylserine, enriched in the cytoplasmic leaflet of mammalian plasma membranes. Circular dichroism spectroscopy revealed that the peptides corresponding to the intracellular third loop (i3) and the C-terminus (C-term) assumed beta-sheet and associated alpha-helical structures, respectively. A structural change was observed when i3 was mixed with C-term, indicating an interaction between them. Fluorescence experiments showed that i3 suppressed the self-association of C-term, confirming the interaction. These results demonstrate for the first time specific interaction between the intracellular third loop and the C-terminus. A model is proposed for the activation of the receptor.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Yano Y,Shimbo T,Sugimoto Y,Matsuzaki Kdoi
10.1016/j.bbrc.2008.04.180subject
Has Abstractpub_date
2008-07-11 00:00:00pages
846-9issue
4eissn
0006-291Xissn
1090-2104pii
S0006-291X(08)00869-3journal_volume
371pub_type
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