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TitleMolecular Basis of 1-Deoxygalactonojirimycin Arylthiourea Binding to Human alpha-Galactosidase A: Pharmacological Chaperoning Efficacy on Fabry Disease Mutants.
Journal, issue, pagesAcs Chem. Biol., Vol. 9, Page 1460-1469, Year 2014
Publish dateDec 9, 2013 (structure data deposition date)
AuthorsYu, Y. / Mena-Barragan, T. / Higaki, K. / Johnson, J.L. / Drury, J.E. / Lieberman, R.L. / Nakasone, N. / Ninomiya, H. / Tsukimura, T. / Sakuraba, H. ...Yu, Y. / Mena-Barragan, T. / Higaki, K. / Johnson, J.L. / Drury, J.E. / Lieberman, R.L. / Nakasone, N. / Ninomiya, H. / Tsukimura, T. / Sakuraba, H. / Suzuki, Y. / Nanba, E. / Mellet, C.O. / Garcia Fernandez, J.M. / Ohno, K.
External linksAcs Chem. Biol. / PubMed:24783948
MethodsX-ray diffraction
Resolution2.5493 Å
Structure data

PDB-4nxs:
Crystal structure of human alpha-galactosidase A in complex with 1-deoxygalactonojirimycin-pFPhT
Method: X-RAY DIFFRACTION / Resolution: 2.5493 Å

Chemicals

ChemComp-SO4:
SULFATE ION

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

ChemComp-2OZ:
(2R,3S,4R,5S)-N-(4-fluorophenyl)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidine-1-carbothioamide

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE/HYDROLASE INHIBITOR / Pharmacological Chaperone / Drug Delivery Systems / Enzyme Activation / Enzyme Stability / Humans / Lysosomes / Molecular Chaperones / Protein Binding / alpha-Galactosidase / Hydrolase-Hydrolase Inhibitor Complex / Fabry Disease / GLA Gene / Arylthiourea

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