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| | <StructureSection load='3miv' size='340' side='right'caption='[[3miv]], [[Resolution|resolution]] 3.50Å' scene=''> | | <StructureSection load='3miv' size='340' side='right'caption='[[3miv]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3miv]] 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=3MIV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3MIV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3miv]] 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=3MIV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MIV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]] 3.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1x1v|1x1v]], [[3mit|3mit]], [[3miu|3miu]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[http://proteopedia.org/fgij/fg.htm?mol=3miv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3miv OCA], [http://pdbe.org/3miv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3miv RCSB], [http://www.ebi.ac.uk/pdbsum/3miv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3miv 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=3miv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3miv OCA], [https://pdbe.org/3miv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3miv RCSB], [https://www.ebi.ac.uk/pdbsum/3miv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3miv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8L5H4_MUSAC Q8L5H4_MUSAC] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Musa acuminata]] | | [[Category: Musa acuminata]] |
| - | [[Category: Sharma, A]] | + | [[Category: Sharma A]] |
| - | [[Category: Vijayan, M]] | + | [[Category: Vijayan M]] |
| - | [[Category: All beta sheet protein]]
| + | |
| - | [[Category: Beta prism-i fold]]
| + | |
| - | [[Category: Mannose specific]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
Function
Q8L5H4_MUSAC
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sharma A, Vijayan M. 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. Glycobiology. 2010 Aug 20. PMID:20729346 doi:10.1093/glycob/cwq128
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