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Crystal Structure of Thioflavin T Bound to the Peripheral Site of Torpedo californica Acetylcholinesterase Reveals How Thioflavin T Acts as a Sensitive Fluorescent Reporter of Ligand Binding to the Acylation Site

Acetylcholinesterase plays a key role in cholinergic synaptic transmission by hydrolyzing the neurotransmitter acetylcholine with one of the highest known catalytic rate constants. Hydrolysis occurs in a narrow and deep gorge that contains two sites of ligand binding: A peripheral site, or P-site, n...

Täydet tiedot

Tallennettuna:
Bibliografiset tiedot
Päätekijät: Harel, Michal, Sonoda, Leilani K., Silman, Israel, Sussman, Joel L., Rosenberry, Terrone L.
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: 2008
Aiheet:
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC3923376/
https://ncbi.nlm.nih.gov/pubmed/18512913
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/ja7109822
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