His145-Trp146 residues and the disulfide-linked loops in atrial natriuretic peptide receptor are critical for the ligand-binding activity.

doi:10.1093/oxfordjournals.jbchem.a124376

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Article

His145-Trp146 residues and the disulfide-linked loops in atrial natriuretic peptide receptor are critical for the ligand-binding activity.

Journal of biochemistry - 1 Mar 1994

Iwashina M, Mizuno T, Hirose S, Ito T, Hagiwara H

Abstract excerpt

To define the ligand-binding site of natriuretic peptide receptor (NPR), amino acid substitutions were carried out by site-directed mutagenesis at selected residues of bovine NPR-C. The mutant receptors were expressed in COS-1 cells and the effect of the mutations on the binding of ligand was analyzed by binding assay, affinity labeling, and immunoblotting. The replacement of His145-Trp146 (HW) by Leu145-Leu146...

Topics

Amino Acid Sequence
Animals
Base Sequence
Binding Sites
Cattle
Cell Line
Disulfides
Histidine
Humans
Immunoblotting
Ligands
Mice

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutagenesis, Site-Directed

Mutation

Rats

Receptors, Atrial Natriuretic Factor

Sequence Homology, Amino Acid

Source

Open in PubMed

Identifiers

PMID: 8056773
DOI: 10.1093/oxfordjournals.jbchem.a124376

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8056773-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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