The classical (acetylcholine) binding sites of all five subtypes of muscarinic receptors are known to be subject to allosteric regulation by a variety of small molecules. The hallmarks of such modulation in binding assays are that the allosteric ligands can alter both the affinities and the rates of
Orthosteric and allosteric binding sites of P2X receptors
β Scribed by R. J. Evans
- Publisher
- Springer
- Year
- 2008
- Tongue
- English
- Weight
- 391 KB
- Volume
- 38
- Category
- Article
- ISSN
- 1432-1017
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During the course of biological function, proteins interact with other proteins, ligands, substrates, inhibitors, etc. These interactions occur at precisely defined locations within the protein but their effects are sometimes propagated to distal regions, triggering highly specific responses. These
In the article cited above, figure 6 on page 199 is incorrect. The residue listed as methionine in the human m1 muscarinic receptor sequence should have been valine and the residue listed as glutamine in the Hm4 sequence should have been histidine. The correct figure is shown below. The author regre