Key result
Monomeric natriuretic peptide receptor-C (NPR-C) contains a high-affinity binding site for natriuretic peptides, and invariant residues Asp407-Arg408 and Asp411-Phe412 are essential for binding.
Population
COS-1 cells expressing C-terminally truncated mutants of natriuretic peptide receptor-C (NPR-C)
Design
Preclinical
Authors
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Does not support clinical translation; leaves open whether these residues enable selective NPR-C modulation in cardiovascular models.
This preclinical study demonstrates that monomeric NPR-C retains high-affinity ligand-binding activity and identifies specific invariant residues essential for this function.
Itakura et al. (1997) studied this question. C-terminally truncated mutants and site-directed mutagenesis of NPR-C was evaluated on Ligand-binding activity. Monomeric natriuretic peptide receptor-C (NPR-C) contains a high-affinity binding site for natriuretic peptides, and invariant residues Asp407-Arg408 and Asp411-Phe412 are essential for binding.
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