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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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A single residue determines the distinct pharmacology of rat and human natriuretic peptide receptor-C.

We report the cloning and expressing of rat natriuretic peptide receptor-C (NPR-C), which binds naturally occurring and synthetic ligands with higher affinity than human NPR-C. Using rat/human hybrids and site-directed mutagenesis, we identified residue 188, Ala for rat and Ile for human, which modulates hormone binding. Orthologous mutagenesis at position 188 for either rNPR-C or hNPR-C results in a complete reversal of the pharmacology. To our knowledge, this is the first example of a single transmembrane domain receptor for which a single residue dictates the ligand binding properties; previous examples are limited to seven transmembrane receptors.[1]

References

  1. A single residue determines the distinct pharmacology of rat and human natriuretic peptide receptor-C. Engel, A.M., Schoenfeld, J.R., Lowe, D.G. J. Biol. Chem. (1994) [Pubmed]
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