Role of the amino terminus in ligand binding for the angiotensin II type 2 receptor

Brain Res Mol Brain Res. 1998 Jun 15;57(2):325-9. doi: 10.1016/s0169-328x(98)00104-1.

Abstract

Key amino terminal residues in type 1 (AT1) angiotensin II (AngII) receptors are not conserved within type 2 (AT2) receptors. We therefore characterized amino terminal mutants that are transiently expressed in COS-3 membranes. AT2 amino terminal deletion drastically reduced affinity for AngII, suggesting its importance for this subtype. AT1-AT2 amino terminal exchanges retained wild type AngII affinities (Kd ranging from 3-5 nM), indicating compensation despite substantial sequence dissimilarities. Finally, binding of AT2 selective ligands (CGP42112A and PD123319) was not dependent on the amino terminus.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Binding, Competitive
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed*
  • Polymerase Chain Reaction
  • Radioligand Assay
  • Receptors, Angiotensin / genetics
  • Receptors, Angiotensin / metabolism*

Substances

  • Receptors, Angiotensin