3mit
From Proteopedia
(Difference between revisions)
m (Protected "3mit" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | + | ==Structure of Banana lectin-alpha-D-mannose complex== | |
| - | + | <StructureSection load='3mit' size='340' side='right' caption='[[3mit]], [[Resolution|resolution]] 2.32Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3mit]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Musa_acuminata Musa acuminata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MIT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MIT FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1x1v|1x1v]], [[3miu|3miu]], [[3miv|3miv]]</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=3mit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mit OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mit RCSB], [http://www.ebi.ac.uk/pdbsum/3mit PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/3mit_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/chain_selection.php?pdb_ID=2ata 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> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Musa acuminata]] | [[Category: Musa acuminata]] | ||
| - | [[Category: Sharma, A | + | [[Category: Sharma, A]] |
| - | [[Category: Vijayan, M | + | [[Category: Vijayan, M]] |
[[Category: All beta sheet protein]] | [[Category: All beta sheet protein]] | ||
[[Category: Beta prism-i fold]] | [[Category: Beta prism-i fold]] | ||
[[Category: Mannose specific]] | [[Category: Mannose specific]] | ||
[[Category: Sugar binding protein]] | [[Category: Sugar binding protein]] | ||
Revision as of 16:18, 21 December 2014
Structure of Banana lectin-alpha-D-mannose complex
| |||||||||||

