6b9o: Difference between revisions
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==Structure of GH 38 Jack Bean alpha-mannosidase== | |||
<StructureSection load='6b9o' size='340' side='right' caption='[[6b9o]], [[Resolution|resolution]] 1.84Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6b9o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B9O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B9O FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-mannosidase Alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.24 3.2.1.24] </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=6b9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b9o OCA], [http://pdbe.org/6b9o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b9o RCSB], [http://www.ebi.ac.uk/pdbsum/6b9o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b9o ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Multivalent design of glycosidase inhibitors is a promising strategy for the treatment of diseases involving enzymatic hydrolysis of glycosidic bonds in carbohydrates. An essential prerequisite for successful applications is the atomic-level understanding of how outstanding binding enhancement occurs with multivalent inhibitors. Herein we report the first high-resolution crystal structures of the Jack bean alpha-mannosidase (JBalpha-man) in apo and inhibited states. The three-dimensional structure of JBalpha-man in complex with the multimeric cyclopeptoid-based inhibitor displaying the largest binding enhancements reported so far provides decisive insight into the molecular mechanisms underlying multivalent effects in glycosidase inhibition. | |||
Structural Basis of Outstanding Multivalent Effects in Jack Bean alpha-Mannosidase Inhibition.,Howard E, Cousido-Siah A, Lepage ML, Schneider JP, Bodlenner A, Mitschler A, Meli A, Izzo I, Alvarez HA, Podjarny A, Compain P Angew Chem Int Ed Engl. 2018 Jul 2;57(27):8002-8006. doi: 10.1002/anie.201801202., Epub 2018 Jun 6. PMID:29722924<ref>PMID:29722924</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6b9o" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Alpha-mannosidase]] | |||
[[Category: Canavalia ensiformis]] | |||
[[Category: Bodlenner, A]] | |||
[[Category: Compain, P]] | |||
[[Category: Cousido-Siah, A]] | [[Category: Cousido-Siah, A]] | ||
[[Category: Howard, E]] | |||
[[Category: Izzo, I]] | [[Category: Izzo, I]] | ||
[[Category: Lepage, M]] | |||
[[Category: Meli, A]] | |||
[[Category: Mitschler, A]] | [[Category: Mitschler, A]] | ||
[[Category: Podjarny, A]] | [[Category: Podjarny, A]] | ||
[[Category: | [[Category: Riccardis, F De]] | ||
[[Category: | [[Category: Hydrolase]] | ||
[[Category: Mannosidase]] | |||
[[Category: Plant protein]] | |||
