Solution structure of intracellular signal-transducing peptide derived from human beta(2)-adrenergic receptor.
The structure of intracellular third loop peptide (betaIII-2: RRSSKFCLKEKKALK) was studied by CD and NMR spectroscopy. According to the CD study, this peptide forms a helix in the TFE solution. The three-dimensional molecular structure in TFE was determined by the 2D (1)H NMR spectroscopy. The structure consists of a positive charge cluster on the C-terminal side of the peptide chain. This part will be an active site of the peptide interacting with the G-protein.
Okuda
Ayumu
A
Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan.
Matsumoto
Osamu
O
Akaji
Masako
M
Taga
Tooru
T
Ohkubo
Tadayasu
T
Kobayashi
Yuji
Y
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D021382:Protein Sorting Signals / Q000502:physiology*; D017433:Protein Structure, Secondary; D018343:Receptors, Adrenergic, beta-2 / Q000737:chemistry*; D015398:Signal Transduction / Q000502:physiology
D010446:Peptide Fragments; D021382:Protein Sorting Signals; D018343:Receptors, Adrenergic, beta-2