Key result
Orthologous mutagenesis at position 188 for either rat or human natriuretic peptide receptor-C results in a complete reversal of the receptor's pharmacology and ligand binding properties.
Population
Rat and human natriuretic peptide receptor-C (NPR-C) models (cloned and expressed)
Comparison
Site-directed mutagenesis at position 188 vs Wild-type receptors
Design
Preclinical
Authors
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Residue 188 dictates NPR-C species pharmacology; extends receptor structural insights but leaves open human therapeutic translation.
A single residue (188) in the natriuretic peptide receptor-C determines the distinct ligand binding pharmacology between rat and human variants, representing the first such finding for a single transmembrane domain receptor.
Engel et al. (1994) studied this question. Orthologous mutagenesis at position 188 was evaluated on Ligand binding properties and pharmacology. Orthologous mutagenesis at position 188 for either rat or human natriuretic peptide receptor-C results in a complete reversal of the receptor's pharmacology and ligand binding properties.
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