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3l4v

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{{Seed}}
 
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[[Image:3l4v.jpg|left|200px]]
 
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<!--
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==Crystal complex of N-terminal Human Maltase-Glucoamylase with kotalanol==
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The line below this paragraph, containing "STRUCTURE_3l4v", creates the "Structure Box" on the page.
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<StructureSection load='3l4v' size='340' side='right' caption='[[3l4v]], [[Resolution|resolution]] 2.10&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'>[[3l4v]] is a 1 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=3L4V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L4V FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KTL:(1S,2R,3R,4S)-1-{(1S)-2-[(2R,3S,4S)-3,4-DIHYDROXY-2-(HYDROXYMETHYL)TETRAHYDROTHIOPHENIUM-1-YL]-1-HYDROXYETHYL}-2,3,4,5-TETRAHYDROXYPENTYL+SULFATE'>KTL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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-->
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3l4t|3l4t]], [[3l4u|3l4u]], [[3l4w|3l4w]], [[3l4x|3l4x]], [[3l4y|3l4y]], [[3l4z|3l4z]]</td></tr>
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{{STRUCTURE_3l4v| PDB=3l4v | SCENE= }}
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MGA, MGAM, MGAML ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<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=3l4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l4v OCA], [http://pdbe.org/3l4v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3l4v RCSB], [http://www.ebi.ac.uk/pdbsum/3l4v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3l4v ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/MGA_HUMAN MGA_HUMAN]] May serve as an alternate pathway for starch digestion when luminal alpha-amylase activity is reduced because of immaturity or malnutrition. May play a unique role in the digestion of malted dietary oligosaccharides used in food manufacturing.
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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/l4/3l4v_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=3l4v 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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An approach to controlling blood glucose levels in individuals with type 2 diabetes is to target alpha-amylases and intestinal glucosidases using alpha-glucosidase inhibitors acarbose and miglitol. One of the intestinal glucosidases targeted is the N-terminal catalytic domain of maltase-glucoamylase (ntMGAM), one of the four intestinal glycoside hydrolase 31 enzyme activities responsible for the hydrolysis of terminal starch products into glucose. Here we present the X-ray crystallographic studies of ntMGAM in complex with a new class of alpha-glucosidase inhibitors derived from natural extracts of Salacia reticulata, a plant used traditionally in Ayuverdic medicine for the treatment of type 2 diabetes. Included in these extracts are the active compounds salacinol, kotalanol, and de-O-sulfonated kotalanol. This study reveals that de-O-sulfonated kotalanol is the most potent ntMGAM inhibitor reported to date (K(i) = 0.03 microM), some 2000-fold better than the compounds currently used in the clinic, and highlights the potential of the salacinol class of inhibitors as future drug candidates.
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===Crystal complex of N-terminal Human Maltase-Glucoamylase with kotalanol===
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New glucosidase inhibitors from an ayurvedic herbal treatment for type 2 diabetes: structures and inhibition of human intestinal maltase-glucoamylase with compounds from Salacia reticulata.,Sim L, Jayakanthan K, Mohan S, Nasi R, Johnston BD, Pinto BM, Rose DR Biochemistry. 2010 Jan 26;49(3):443-51. PMID:20039683<ref>PMID:20039683</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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<!--
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_20039683}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3l4v" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20039683 is the PubMed ID number.
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== References ==
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-->
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<references/>
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{{ABSTRACT_PUBMED_20039683}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Human]]
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3L4V is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L4V OCA].
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[[Category: Rose, D R]]
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[[Category: Sim, L]]
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==Reference==
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<ref group="xtra">PMID:20039683</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
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[[Category: Rose, D R.]]
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[[Category: Sim, L.]]
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[[Category: Cell membrane]]
[[Category: Cell membrane]]
[[Category: Disulfide bond]]
[[Category: Disulfide bond]]
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[[Category: Sulfation]]
[[Category: Sulfation]]
[[Category: Transmembrane]]
[[Category: Transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 10 17:25:21 2010''
 

Current revision

Crystal complex of N-terminal Human Maltase-Glucoamylase with kotalanol

3l4v, resolution 2.10Å

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