5emy: Difference between revisions
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==Human Pancreatic Alpha-Amylase in complex with the mechanism based inactivator glucosyl epi-cyclophellitol== | |||
<StructureSection load='5emy' size='340' side='right' caption='[[5emy]], [[Resolution|resolution]] 1.23Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5emy]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EMY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EMY FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5QP:(2~{R},3~{S},4~{S},5~{R},6~{S})-2-(HYDROXYMETHYL)-6-[(1~{R},2~{S},3~{R},5~{S},6~{R})-2-(HYDROXYMETHYL)-3,5,6-TRIS(OXIDANYL)CYCLOHEXYL]OXY-OXANE-3,4,5-TRIOL'>5QP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | |||
<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> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4x9y|4x9y]], [[4w93|4w93]], [[1cpu|1cpu]]</td></tr> | |||
<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> | |||
<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=5emy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5emy OCA], [http://pdbe.org/5emy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5emy RCSB], [http://www.ebi.ac.uk/pdbsum/5emy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5emy ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
As part of a search for selective, mechanism-based covalent inhibitors of human pancreatic alpha-amylase we describe the chemoenzymatic synthesis of the disaccharide analog alpha-glucosyl epi-cyclophellitol, demonstrate its stoichiometric reaction with human pancreatic alpha-amylase and evaluate the time dependence of its inhibition. X-ray crystallographic analysis of the covalent derivative so formed confirms its reaction at the active site with formation of a covalent bond to the catalytic nucleophile D197. The structure illuminates the interactions with the active site and confirms OH4' on the nonreducing end sugar as a good site for attachment of fluorescent tags in generating probes for localization and quantitation of amylase in vivo. | |||
Glucosyl epi-cyclophellitol allows mechanism-based inactivation and structural analysis of human pancreatic alpha-amylase.,Caner S, Zhang X, Jiang J, Chen HM, Nguyen NT, Overkleeft H, Brayer GD, Withers SG FEBS Lett. 2016 Apr;590(8):1143-51. doi: 10.1002/1873-3468.12143. Epub 2016 Apr, 3. PMID:27000970<ref>PMID:27000970</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5emy" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Alpha-amylase]] | |||
[[Category: Brayer, G D]] | |||
[[Category: Caner, S]] | [[Category: Caner, S]] | ||
[[Category: | [[Category: Amylase]] | ||
[[Category: Diabetes]] | |||
[[Category: Glucosyl hydrolase]] | |||
[[Category: Hydrolase-hydrolase inhibitor complex]] | |||
[[Category: Obesity]] | |||
Revision as of 02:20, 13 July 2016
Human Pancreatic Alpha-Amylase in complex with the mechanism based inactivator glucosyl epi-cyclophellitol
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