3mit: Difference between revisions
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==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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3MIT 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]] 2.32Å</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=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=3mit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mit OCA], [https://pdbe.org/3mit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mit RCSB], [https://www.ebi.ac.uk/pdbsum/3mit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mit 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/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/main_output.php?pdb_ID=3mit 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> | |||
<div class="pdbe-citations 3mit" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Musa acuminata]] | |||
[[Category: Sharma A]] | |||
[[Category: Vijayan M]] | |||
Latest revision as of 19:34, 1 November 2023
Structure of Banana lectin-alpha-D-mannose complexStructure of Banana lectin-alpha-D-mannose complex
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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