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==X-ray structure of a conjugate with conduritol-beta-epoxide of acid-beta-glucosidase overexpressed in cultured plant cells== | ==X-ray structure of a conjugate with conduritol-beta-epoxide of acid-beta-glucosidase overexpressed in cultured plant cells== | ||
<StructureSection load='2vt0' size='340' side='right' caption='[[2vt0]], [[Resolution|resolution]] 2.15Å' scene=''> | <StructureSection load='2vt0' size='340' side='right' caption='[[2vt0]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2vt0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VT0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VT0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2vt0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VT0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VT0 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CBU:(1R,2R,3S,4S,5S,6S)-CYCLOHEXANE-1,2,3,4,5,6-HEXOL'>CBU | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CBU:(1R,2R,3S,4S,5S,6S)-CYCLOHEXANE-1,2,3,4,5,6-HEXOL'>CBU</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucosylceramidase Glucosylceramidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.45 3.2.1.45] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucosylceramidase Glucosylceramidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.45 3.2.1.45] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vt0 OCA], [http://pdbe.org/2vt0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vt0 RCSB], [http://www.ebi.ac.uk/pdbsum/2vt0 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vt0 OCA], [http://pdbe.org/2vt0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vt0 RCSB], [http://www.ebi.ac.uk/pdbsum/2vt0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vt0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 11: | Line 12: | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vt/2vt0_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vt/2vt0_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
| Line 43: | Line 44: | ||
[[Category: Sussman, J L]] | [[Category: Sussman, J L]] | ||
[[Category: Alternative initiation]] | [[Category: Alternative initiation]] | ||
[[Category: Alternative splicing]] | |||
[[Category: Cerezyme]] | [[Category: Cerezyme]] | ||
[[Category: Disease mutation]] | [[Category: Disease mutation]] | ||
| Line 55: | Line 57: | ||
[[Category: Lysosome]] | [[Category: Lysosome]] | ||
[[Category: Membrane]] | [[Category: Membrane]] | ||
[[Category: Pharmaceutical]] | |||
[[Category: Polymorphism]] | |||
[[Category: Sphingolipid metabolism]] | [[Category: Sphingolipid metabolism]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
Revision as of 00:16, 20 September 2018
X-ray structure of a conjugate with conduritol-beta-epoxide of acid-beta-glucosidase overexpressed in cultured plant cellsX-ray structure of a conjugate with conduritol-beta-epoxide of acid-beta-glucosidase overexpressed in cultured plant cells
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn mammalian cells, glucosylceramide (GlcCer), the simplest glycosphingolipid, is hydrolyzed by the lysosomal enzyme acid beta-glucosidase (GlcCerase). In the human metabolic disorder Gaucher disease, GlcCerase activity is significantly decreased owing to one of approximately 200 mutations in the GlcCerase gene. The most common therapy for Gaucher disease is enzyme replacement therapy (ERT), in which patients are given intravenous injections of recombinant human GlcCerase; the Genzyme product Cerezyme has been used clinically for more than 15 years and is administered to approximately 4000 patients worldwide. Here we review the crystal structure of Cerezyme and other recombinant forms of GlcCerase, as well as of their complexes with covalent and non-covalent inhibitors. We also discuss the stability of Cerezyme, which can be altered by modification of its N-glycan chains with possible implications for improved ERT in Gaucher disease. Acid beta-glucosidase: insights from structural analysis and relevance to Gaucher disease therapy.,Kacher Y, Brumshtein B, Boldin-Adamsky S, Toker L, Shainskaya A, Silman I, Sussman JL, Futerman AH Biol Chem. 2008 Nov;389(11):1361-9. PMID:18783340[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Glucosylceramidase
- Human
- Aviezer, D
- Brumshtein, B
- Futerman, A H
- Greenblatt, H M
- Shaaltiel, Y
- Silman, I
- Sussman, J L
- Alternative initiation
- Alternative splicing
- Cerezyme
- Disease mutation
- Gaucher disease
- Glucocerebrosidase
- Glucosidase
- Glycoprotein
- Glycosidase
- Hydrolase
- ISPC, Israel Structural Proteomics Center
- Lipid metabolism
- Lysosome
- Membrane
- Pharmaceutical
- Polymorphism
- Sphingolipid metabolism
- Structural genomic