Solution structure of intracellular signal-transducing peptide derived from human beta(2)-adrenergic receptor

Biochem Biophys Res Commun. 2002 Mar 15;291(5):1297-301. doi: 10.1006/bbrc.2002.6606.

Abstract

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.

MeSH terms

  • Amino Acid Sequence
  • Circular Dichroism
  • Humans
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Protein Sorting Signals / physiology*
  • Protein Structure, Secondary
  • Receptors, Adrenergic, beta-2 / chemistry*
  • Signal Transduction / physiology

Substances

  • Peptide Fragments
  • Protein Sorting Signals
  • Receptors, Adrenergic, beta-2