NDLI: Differentiation between binding sites for angiotensin II and nonpeptide antagonists on the angiotensin II type 1 receptors.

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Differentiation between binding sites for angiotensin II and nonpeptide antagonists on the angiotensin II type 1 receptors.

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Differentiation between binding sites for angiotensin II and nonpeptide antagonists on the angiotensin II type 1 receptors.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Hjorth, S. A. Bergsma, D. J. Schwartz, T. W. Schambye, H. T. Sathe, G.
Description	Author Affiliation: Schambye HT ( University Department of Clinical Biochemistry, Rigshospitalet, Copenhagen, Denmark.);
Abstract	To characterize binding sites for nonpeptide angiotensin antagonists on the human angiotensin II receptor type 1 (AT1 receptor) we have systematically exchanged segments of the human receptor with corresponding segments from a homologous Xenopus laevis receptor, which does not bind the nonpeptide compounds. Substitution of transmembrane segment VII of the human AT1 receptor dramatically reduced the binding affinity of all of the 11 nonpeptide antagonists tested (55- to > 2000-fold) with no effect on the binding of angiotensin. The affinity for the nonpeptide compounds decreased additionally one order of magnitude when transmembrane segment VI and the connecting extracellular loop 3 from the Xenopus receptor were also introduced into the human AT1 receptor. Exchanges of smaller segments and single residues in transmembrane segments VI and VII and extracellular loop 3 revealed that the binding of nonpeptide antagonists was dependent on nonconserved residues located deep within the transmembrane segments VI and VII, in particular Asn295 in transmembrane segment VII. Surprisingly, all exchanges in transmembrane segment VII, including the Asn295 to Ser substitution, had a more pronounced effect on the binding of the competitive antagonists relative to the insurmountable antagonists. It is concluded that the binding mode for peptide and nonpeptide ligands on the AT1 receptor is rather different and that competitive and insurmountable antagonists presumably bind to overlapping but distinct sites located in transmembrane segments VI and VII.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	15
Volume Number	91
Language	English
Publisher	National Academy of Sciences
Publisher Date	1994-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Angiotensin II Metabolism Angiotensin Receptor Antagonists Amino Acid Sequence Animals Binding Sites Molecular Sequence Data Molecular Structure Mutation Peptides Receptors, Angiotensin Xenopus Laevis Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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