View source for 6tbg


==Structure of a beta galactosidase with inhibitor==
<StructureSection load='6tbg' size='340' side='right'caption='[[6tbg]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6tbg]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellvibrio_japonicus_Ueda107 Cellvibrio japonicus Ueda107]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TBG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=N0N:5-(dimethylamino)-~{N}-[6-[[(1~{R},2~{R},3~{S},4~{S},5~{S})-2-(hydroxymethyl)-3,4,5-tris(oxidanyl)cyclopentyl]amino]hexyl]naphthalene-1-sulfonamide'>N0N</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6tbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tbg OCA], [https://pdbe.org/6tbg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tbg RCSB], [https://www.ebi.ac.uk/pdbsum/6tbg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tbg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B3PBE0_CELJU B3PBE0_CELJU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glycosidase inhibitors have shown great potential as pharmacological chaperones for lysosomal storage diseases. In light of this, a series of new cyclopentanoid beta-galactosidase inhibitors were prepared and their inhibitory and pharmacological chaperoning activities determined and compared with those of lipophilic analogs of the potent beta-d-galactosidase inhibitor 4-epi-isofagomine. Structure-activity relationships were investigated by X-ray crystallography as well as by alterations in the cyclopentane moiety such as deoxygenation and replacement by fluorine of a "strategic" hydroxyl group. New compounds have revealed highly promising activities with a range of beta-galactosidase-compromised human cell lines and may serve as leads towards new pharmacological chaperones for GM1-gangliosidosis and Morquio B disease.

Mechanistic Insights into the Chaperoning of Human Lysosomal-Galactosidase Activity: Highly Functionalized Aminocyclopentanes and C-5a-Substituted Derivatives of 4-epi-Isofagomine.,Weber P, Thonhofer M, Averill S, Davies GJ, Santana AG, Muller P, Nasseri SA, Offen WA, Pabst BM, Paschke E, Schalli M, Torvisco A, Tschernutter M, Tysoe C, Windischhofer W, Withers SG, Wolfsgruber A, Wrodnigg TM, Stutz AE Molecules. 2020 Sep 3;25(17). pii: molecules25174025. doi:, 10.3390/molecules25174025. PMID:32899288<ref>PMID:32899288</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6tbg" style="background-color:#fffaf0;"></div>

==See Also==
*[[Galactosidase 3D structures|Galactosidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cellvibrio japonicus Ueda107]]
[[Category: Large Structures]]
[[Category: Davies G]]
[[Category: Offen W]]