6z8l
From Proteopedia
(Difference between revisions)
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<StructureSection load='6z8l' size='340' side='right'caption='[[6z8l]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='6z8l' size='340' side='right'caption='[[6z8l]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Z8L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Z8L FirstGlance]. <br> |
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4000037Å</td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4000037Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene></td></tr> | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</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=6z8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6z8l OCA], [https://pdbe.org/6z8l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6z8l RCSB], [https://www.ebi.ac.uk/pdbsum/6z8l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6z8l ProSAT]</span></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=6z8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6z8l OCA], [https://pdbe.org/6z8l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6z8l RCSB], [https://www.ebi.ac.uk/pdbsum/6z8l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6z8l ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == Function == | ||
| - | [https://www.uniprot.org/uniprot/AMYP_HUMAN AMYP_HUMAN] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Single site OH --> F substitution at the termini of maltotetraose leads to significantly improved hydrolytic stability towards alpha-amylase and alpha-glucosidase relative to the natural compound. To explore the effect of molecular editing, selectively modified oligosaccharides were prepared via a convergent alpha-selective strategy. Incubation experiments in purified alpha-amylase and alpha-glucosidase, and in human and murine blood serum, provide insight into the influence of fluorine on the hydrolytic stability of these clinically important scaffolds. Enhancements of ca. 1 order of magnitude result from these subtle single point mutations. Modification at the monosaccharide furthest from the probable enzymatic cleavage termini leads to the greatest improvement in stability. In the case of alpha-amylase, docking studies revealed that retentive C2-fluorination at the reducing end inverts the orientation in which the substrate is bound. A co-crystal structure of human alpha-amylase revealed maltose units bound at the active-site. In view of the evolving popularity of C(sp(3))-F bioisosteres in medicinal chemistry, and the importance of maltodextrins in bacterial imaging, this discovery begins to reconcile the information-rich nature of carbohydrates with their intrinsic hydrolytic vulnerabilities. | ||
| - | |||
| - | Enhancing glycan stability via site-selective fluorination: modulating substrate orientation by molecular design.,Axer A, Jumde RP, Adam S, Faust A, Schafers M, Fobker M, Koehnke J, Hirsch AKH, Gilmour R Chem Sci. 2020 Nov 23;12(4):1286-1294. doi: 10.1039/d0sc04297h. PMID:34163891<ref>PMID:34163891</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 6z8l" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Amylase 3D structures|Amylase 3D structures]] | *[[Amylase 3D structures|Amylase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Adam S]] | [[Category: Adam S]] | ||
[[Category: Koehnke J]] | [[Category: Koehnke J]] | ||
Current revision
Alpha-Amylase in complex with probe fragments
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