Title : Allosteric modulation of acetylcholinesterase activity by peripheral ligands involves a conformational transition of the anionic subsite.

Pub. Date : 1995 Nov 28

PMID : 7492545






1 Functional Relationships(s)
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1 Replacement of residues Asp74, Trp286, and Tyr72, which are constituents of the peripheral anionic site (PAS) of human acetylcholinesterase (HuAChE), affected similarly both the binding and the inhibition constants of the PAS-specific ligand propidium, demonstrating that changes in the inhibitory activity are a direct consequence of altered binding to the PAS. Propidium acetylcholinesterase (Cartwright blood group) Homo sapiens