Key result
Mutating residues 188 and 205 in NPR-C tightens human ligand binding but weakens rat binding.
Population
Rat and human natriuretic peptide clearance receptor (NPR-C)
Design
Preclinical
Authors
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Species differences in NPR-C affinity require caution extrapolating rodent data to humans; extends mapping of residues modulating ligand binding.
Identifies key residues in the extracellular domain of NPR-C that modulate ligand binding affinity, providing insight into receptor pharmacology.
Engel et al. (1995) studied this question. Mutagenesis of residues 188 and 205 in NPR-C vs. Wild-type receptor was evaluated on Hormone binding affinity. Orthologous mutation of residues 188 and 205 in the natriuretic peptide clearance receptor modulates ligand affinity, resulting in tighter binding for human and weaker binding for rat NPR-C.
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