Article
Conversion of antagonist-binding site to metal-ion site in the tachykinin NK-1 receptor.
Nature - 2 Mar 1995
Elling C E, Nielsen S M, Schwartz T W
Abstract excerpt
Mutational analysis of the tachykinin NK-1 (refs 1-7), NK-2 (ref. 8) and angiotensin AT-1 (refs 9, 10) receptors indicates that non-peptide antagonists act through residues located between the seven transmembrane segments, whereas natural peptide agonists bind mainly to residues scattered in the exterior part of the receptor. The presumed contact points for the prototype NK-1 antagonist CP96,345 cluster on...
Topics
- Allosteric Regulation
- Amino Acid Sequence
- Binding Sites
- Biphenyl Compounds
- Cell Line
- Copper
- Histidine
- Humans
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Neurokinin-1 Receptor Antagonists