Sandbox Reserved 475: Difference between revisions

As shown in the picture to the right, rendered using electron microscopy to show the two α-subunits are colored orange in this homeric receptor example. The two α-subunits each contain a ligand binding site colored red. '''Cys-192''' and '''Cys-193''', which are close proximity to the allosteric binding sites on the α-subunits for acetylcholine have been experimentally tested to show that disulfide residues provides stability in the binding of the neurotransmitter.<ref name="Refined"/> The image (bottom left) shows a simplified depiction of the main components of one of the binding sites in a nAChR. Acetylcholine is shown to interact with various amino acid residues but specifically with the series of amino acids: Tyrosine (Y), Cysteine (C), Cysteine (C), and Tyrosine (Y). The cysteine sulfide residues form the disulfide interaction which aids in acetylcholine binding. The disulfide bonds facilitate the loop formations necessary for the appropriate bonds being formed with acetylcholine.