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-Structure paper
Title | Molecular Basis of 1-Deoxygalactonojirimycin Arylthiourea Binding to Human alpha-Galactosidase A: Pharmacological Chaperoning Efficacy on Fabry Disease Mutants. |
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Journal, issue, pages | Acs Chem. Biol., Vol. 9, Page 1460-1469, Year 2014 |
Publish date | Dec 9, 2013 (structure data deposition date) |
![]() | Yu, 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. |
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Methods | X-ray diffraction |
Resolution | 2.5493 Å |
Structure data | ![]() PDB-4nxs: |
Chemicals | ![]() ChemComp-SO4: ![]() ChemComp-NAG: ![]() ChemComp-2OZ: ![]() ChemComp-HOH: |
Source |
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![]() | HYDROLASE/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 |