Identification of the gamma-subunit interaction sites in the retinal cyclic-GMP phosphodiesterase beta-subunit

Biochem Biophys Res Commun. 1991 Jul 31;178(2):474-9. doi: 10.1016/0006-291x(91)90131-p.

Abstract

Using synthetic peptides, the identification of the retinal cyclic-GMP phosphodiesterase (cGMP PDE) interaction sites for the inhibitory gamma-subunit in the catalytic alpha-subunit were recently localized to residues #16-30 and 78-90 in the alpha-subunit (1). In this study, a binding radioimmunoassay (RIA) showed a weak interaction between PDE gamma and PDE beta subunits in PDE beta residues #15-34, and stronger interaction sites were found in residues #91-110 and 211-230. Sequence comparison between PDE alpha and PDE beta illustrate some differences in these regions, particularly in PDE alpha 16-30 and PDE beta 15-34 regions. Differences in interaction sites in PDE alpha and PDE beta for PDE gamma may account for the differences in affinities observed between PDE gamma and the catalytic subunits.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 3',5'-Cyclic-GMP Phosphodiesterases / chemistry
  • 3',5'-Cyclic-GMP Phosphodiesterases / metabolism*
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cattle
  • Immune Sera
  • Macromolecular Substances
  • Molecular Sequence Data
  • Radioimmunoassay
  • Rod Cell Outer Segment / enzymology*

Substances

  • Immune Sera
  • Macromolecular Substances
  • 3',5'-Cyclic-GMP Phosphodiesterases