3miu
From Proteopedia
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| - | {{STRUCTURE_3miu| PDB=3miu | SCENE= }} | ||
| - | ===Structure of Banana Lectin-pentamannose complex=== | ||
| - | {{ABSTRACT_PUBMED_20729346}} | ||
| - | == | + | ==Structure of Banana Lectin-pentamannose complex== |
| - | [[3miu]] is a 2 chain structure with sequence from [ | + | <StructureSection load='3miu' size='340' side='right'caption='[[3miu]], [[Resolution|resolution]] 2.63Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3miu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Musa_acuminata Musa acuminata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MIU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MIU 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]] 2.63Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=PRD_900112:3alpha-alpha-mannobiose'>PRD_900112</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3miu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3miu OCA], [https://pdbe.org/3miu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3miu RCSB], [https://www.ebi.ac.uk/pdbsum/3miu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3miu ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q8L5H4_MUSAC Q8L5H4_MUSAC] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mi/3miu_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3miu ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The three crystal structures reported here provide details of the interactions of mannose and the mannosyl-alpha-1,3-mannose component of a pentamannose with banana lectin and evidence for the binding of glucosyl-alpha-1,2-glucose to the lectin. The known structures involving the lectin include a complex with glucosyl-beta-1,3-glucose. Modelling studies on the three disaccharide complexes with the reducing end and the non-reducing end at the primary binding site are also provided here. The results of the X-ray and modelling studies show that the disaccharides with an alpha-1,3 linkage prefer to have the non-reducing end at the primary binding site while the reducing end is preferred at the site when the linkage is beta-1,3 in mannose/glucose specific beta-prism I fold lectins. In the corresponding galactose-specific lectins, however, alpha-1,3 linked disaccharides cannot bind the lectin with the non-reducing end at the primary binding site on account of steric clashes with an aromatic residue which occurs only when the lectin is galactose-specific. Molecular dynamics simulations based on the known structures involving banana lectin enrich the information on lectin-carbohydrate interactions obtained from crystal structures. They demonstrate that conformational selection as well as induced fit operate when carbohydrates bind to banana lectin. | ||
| - | + | Influence of glycosidic linkage on the nature of carbohydrate binding in {beta}-prism I fold lectins. An X-ray and molecular dynamics investigation on banana lectin - carbohydrate complexes.,Sharma A, Vijayan M Glycobiology. 2010 Aug 20. PMID:20729346<ref>PMID:20729346</ref> | |
| - | <ref | + | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3miu" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Musa acuminata]] | [[Category: Musa acuminata]] | ||
| - | [[Category: Sharma | + | [[Category: Sharma A]] |
| - | [[Category: Vijayan | + | [[Category: Vijayan M]] |
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Current revision
Structure of Banana Lectin-pentamannose complex
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