4w93

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==Human pancreatic alpha-amylase in complex with montbretin A==
==Human pancreatic alpha-amylase in complex with montbretin A==
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<StructureSection load='4w93' size='340' side='right' caption='[[4w93]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
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<StructureSection load='4w93' size='340' side='right'caption='[[4w93]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4w93]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W93 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4W93 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4w93]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W93 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4W93 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3L9:MONTBRETIN+A'>3L9</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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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]] 1.352&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></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=3L9:MONTBRETIN+A'>3L9</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bsi|1bsi]], [[1hny|1hny]], [[1cpu|1cpu]], [[4gqr|4gqr]], [[4gqq|4gqq]]</td></tr>
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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=4w93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w93 OCA], [https://pdbe.org/4w93 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4w93 RCSB], [https://www.ebi.ac.uk/pdbsum/4w93 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4w93 ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] </span></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=4w93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w93 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4w93 RCSB], [http://www.ebi.ac.uk/pdbsum/4w93 PDBsum]</span></td></tr>
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</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AMYP_HUMAN AMYP_HUMAN]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The complex plant flavonol glycoside montbretin A is a potent (Ki = 8 nM) and specific inhibitor of human pancreatic alpha-amylase with potential as a therapeutic for diabetes and obesity. Controlled degradation studies on montbretin A, coupled with inhibition analyses, identified an essential high-affinity core structure comprising the myricetin and caffeic acid moieties linked via a disaccharide. X-ray structural analyses of the montbretin A-human alpha-amylase complex confirmed the importance of this core structure and revealed a novel mode of glycosidase inhibition wherein internal pi-stacking interactions between the myricetin and caffeic acid organize their ring hydroxyls for optimal hydrogen bonding to the alpha-amylase catalytic residues D197 and E233. This novel inhibitory motif can be reproduced in a greatly simplified analog, offering potential for new strategies for glycosidase inhibition and therapeutic development.
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The amylase inhibitor montbretin A reveals a new glycosidase inhibition motif.,Williams LK, Zhang X, Caner S, Tysoe C, Nguyen NT, Wicki J, Williams DE, Coleman J, McNeill JH, Yuen V, Andersen RJ, Withers SG, Brayer GD Nat Chem Biol. 2015 Jul 27. doi: 10.1038/nchembio.1865. PMID:26214255<ref>PMID:26214255</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 4w93" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Amylase 3D structures|Amylase 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Alpha-amylase]]
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[[Category: Homo sapiens]]
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[[Category: Brayer, G D]]
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[[Category: Large Structures]]
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[[Category: Caner, S]]
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[[Category: Brayer GD]]
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[[Category: Williams, L K]]
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[[Category: Caner S]]
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[[Category: Amylase]]
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[[Category: Williams LK]]
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[[Category: Diabetes]]
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[[Category: Enzyme inhibitor]]
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[[Category: Glucosyl hydrolase]]
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Current revision

Human pancreatic alpha-amylase in complex with montbretin A

PDB ID 4w93

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