Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1939684 | Biochemical and Biophysical Research Communications | 2006 | 5 Pages |
Abstract
We found that a peptide (EP3a: TIKALVSRCRAKAAV) corresponding to the N-terminal site of the intracellular third loop of human prostaglandin EP3α receptor could activate G protein α-subunit directly. The activity was almost same as Mastoparan-X, a G protein activating peptide from wasp venom. The three-dimensional molecular structure of the peptide in SDS-d25 micelles was determined by 2D 1H NMR spectroscopy. The structure of EP3a consists of a positive charge cluster on the C-terminal helical site. The cluster was also found in several corresponding receptor peptides. Therefore, the positive charge cluster on the helical structure might play a crucial role in activation of G protein.
Keywords
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Tatsuhiko Kikkou, Osamu Matsumoto, Tadayasu Ohkubo, Yuji Kobayashi, Gozoh Tsujimoto,