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Structure paper

TitleCrystal 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.
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 130, Page 7856-7861, Year 2008
Publish dateAug 23, 2006 (structure data deposition date)
AuthorsHarel, M. / Sonoda, L.K. / Silman, I. / Sussman, J.L. / Rosenberry, T.L.
External linksJ. Am. Chem. Soc. / PubMed:18512913
MethodsX-ray diffraction
Resolution2.8 Å
Structure data

PDB-2j3q:
Torpedo acetylcholinesterase complexed with fluorophore thioflavin T
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-TFL:
2-[4-(DIMETHYLAMINO)PHENYL]-6-HYDROXY-3-METHYL-1,3-BENZOTHIAZOL-3-IUM

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • torpedo californica (Pacific electric ray)
KeywordsHYDROLASE / SERINE ESTERASE / ALTERNATIVE SPLICING / LIPOPROTEIN / GLYCOPROTEIN / TORPEDO ACHE / NEUROTRANSMITTER DEGRADATION / ANTICANCER PRODRUG CPT- 11 / SYNAPSE / MEMBRANE / GPI-ANCHOR

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