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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...

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

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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