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==Human Pancreatic Alpha-Amylase in complex with the mechanism based inactivator glucosyl epi-cyclophellitol== | ==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=''> | <StructureSection load='5emy' size='340' side='right'caption='[[5emy]], [[Resolution|resolution]] 1.23Å' scene=''> | ||
== Structural highlights == | == 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 [ | <table><tr><td colspan='2'>[[5emy]] 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=5EMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.231Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5emy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5emy OCA], [https://pdbe.org/5emy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5emy RCSB], [https://www.ebi.ac.uk/pdbsum/5emy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5emy ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/AMYP_HUMAN AMYP_HUMAN] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 19: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 5emy" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5emy" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Amylase 3D structures|Amylase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Brayer GD]] | ||
[[Category: | [[Category: Caner S]] | ||
Latest revision as of 11:07, 12 July 2023
Human Pancreatic Alpha-Amylase in complex with the mechanism based inactivator glucosyl epi-cyclophellitolHuman Pancreatic Alpha-Amylase in complex with the mechanism based inactivator glucosyl epi-cyclophellitol
Structural highlights
FunctionPublication Abstract from PubMedAs 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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