Crystal Structure of Human Acetylcholinesterase Guides Drug Design
NYSBC crystallographers developed a novel platform for human acetylcholinesterase that allowed binding of ligands to this key enzyme that is necessary for the proper functioning of the nervous system. This patented work allows researchers to explore the critical changes at the binding site of the native enzyme.
X-ray crystal structures of dihydrotanshinone I and territrem B bound to human acetylcholinesterase reveal a wealth of detail about compound-protein interactions, which can be used to design superior drugs to treat nerve agent poisoning. Territrem B traps the enzyme in a unique conformation that has not been observed before.
Research Article: Cheung et al. J Mol Neurosci. online, Feb 2014