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3dx3

From Proteopedia

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{{Seed}}
 
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[[Image:3dx3.jpg|left|200px]]
 
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==Golgi alpha-Mannosidase II in complex with Mannostatin analog (1R,2R,3S,4R,5R)-5-aminocyclopentane-1,2,3,4-tetraol==
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The line below this paragraph, containing "STRUCTURE_3dx3", creates the "Structure Box" on the page.
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<StructureSection load='3dx3' size='340' side='right'caption='[[3dx3]], [[Resolution|resolution]] 1.42&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3dx3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DX3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DX3 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.42&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=YTB:(1R,2R,3S,4R,5R)-5-AMINOCYCLOPENTANE-1,2,3,4-TETROL'>YTB</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_3dx3| PDB=3dx3 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3dx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dx3 OCA], [https://pdbe.org/3dx3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dx3 RCSB], [https://www.ebi.ac.uk/pdbsum/3dx3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dx3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MAN2_DROME MAN2_DROME] Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dx/3dx3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3dx3 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Mannostatin A is a potent inhibitor of the mannose-trimming enzyme, Golgi alpha-mannosidase II (GMII), which acts late in the N-glycan processing pathway. Inhibition of this enzyme provides a route to blocking the transformation-associated changes in cancer cell surface oligosaccharide structures. Here, we report on the synthesis of new Mannostatin derivatives and analyze their binding in the active site of Drosophila GMII by X-ray crystallography. The results indicate that the interaction with the backbone carbonyl of Arg876 is crucial to the high potency of the inhibitor-an effect enhanced by the hydrophobic interaction between the thiomethyl group and an aromatic pocket vicinal to the cleavage site. The various structures indicate that differences in the hydration of protein-ligand complexes are also important determinants of plasticity as well as selectivity of inhibitor binding.
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===Golgi alpha-Mannosidase II in complex with Mannostatin analog (1R,2R,3S,4R,5R)-5-aminocyclopentane-1,2,3,4-tetraol===
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The molecular basis of inhibition of Golgi alpha-mannosidase II by mannostatin A.,Kuntz DA, Zhong W, Guo J, Rose DR, Boons GJ Chembiochem. 2009 Jan 26;10(2):268-77. PMID:19101978<ref>PMID:19101978</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3dx3" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19101978}}, adds the Publication Abstract to the page
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*[[Mannosidase 3D structures|Mannosidase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19101978 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19101978}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3DX3 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DX3 OCA].
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==Reference==
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<ref group="xtra">PMID:19101978</ref><references group="xtra"/>
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[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
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[[Category: Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase]]
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[[Category: Large Structures]]
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[[Category: Kuntz, D A.]]
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[[Category: Kuntz DA]]
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[[Category: Rose, D R.]]
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[[Category: Rose DR]]
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[[Category: Gh38 glycosidase]]
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[[Category: Glycosidase]]
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[[Category: Golgi apparatus]]
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[[Category: Hydrolase]]
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[[Category: Membrane]]
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[[Category: Metal-binding]]
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[[Category: Signal-anchor]]
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[[Category: Transmembrane]]
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[[Category: Zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 8 09:25:23 2009''
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Current revision

Golgi alpha-Mannosidase II in complex with Mannostatin analog (1R,2R,3S,4R,5R)-5-aminocyclopentane-1,2,3,4-tetraol

PDB ID 3dx3

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