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Greenfeder, S. et al.

Greenfeder, Cheewatrakoolpong, Anthes, Billah, Egan, Brown, Murgolo,

Two related neurokinin-1 receptor antagonists have overlapping but different binding sites.

The neuropeptide substance P binds to the G protein- coupled neurokinin-1 ( NK-1) receptor and elicits cellular responses thought to be involved in pain, neurogenic inflammation, vasodilatation, and plasma exudation. Several small molecule nonpeptide antagonists of the substance P/NK-1 receptor interaction have been developed. Mutational analysis of the receptor protein sequence has led to the conclusion that the binding site for these nonpeptide antagonists lies within the bundle created by transmembrane domains IV-VII of the receptor. This current investigation employs site directed mutagenesis of the NK-1 receptor to compare the binding site of CP-96,345 with that of a related compound CP-99,994. The data demonstrate that while both compounds appear to bind within the transmembrane domain bundle, the contribution of individual amino acid residues to the binding of each compound differs.[1]

References

Two related neurokinin-1 receptor antagonists have overlapping but different binding sites. Greenfeder, S., Cheewatrakoolpong, B., Anthes, J., Billah, M., Egan, R.W., Brown, J.E., Murgolo, N.J. Bioorg. Med. Chem. (1998) [Pubmed]

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