7ded
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 7ded is ON HOLD Authors: Sivaji, N., Surolia, A., Vijayan, M. Description: Mevo lectin complex with mannoheptaose (Man7) [[Category: Unreleased Str...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Mevo lectin complex with mannoheptose (Man7)== | |
| + | <StructureSection load='7ded' size='340' side='right'caption='[[7ded]], [[Resolution|resolution]] 2.23Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7ded]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanococcus_voltae_A3 Methanococcus voltae A3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DED 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]] 2.228Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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=7ded FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ded OCA], [https://pdbe.org/7ded PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ded RCSB], [https://www.ebi.ac.uk/pdbsum/7ded PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ded ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/D7DTD6_METV3 D7DTD6_METV3] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Mannose-binding lectins can specifically recognize and bind complex glycan structures on pathogens and have potential as anti-viral and anti-bacterial agents. We previously reported the structure of a lectin from an archaeal species, Mevo lectin, which has specificity towards terminal alpha1,2 linked manno-oligosaccharides. Mycobacterium tuberculosis (M. tuberculosis) expresses mannosylated structures including, lipoarabinomannan (ManLAM) on its surface and exploits C-type lectins to gain entry into the host cells. ManLAM structure has mannose capping with terminal alphaMan(1,2)alphaMan residues and is important for recognition by innate immune cells. Here, we aim to address the specificity of Mevo lectin towards high-mannose type glycans with terminal alphaMan(1,2)alphaMan residues and its effect on M. tuberculosis internalization by macrophages. ITC studies demonstrated that Mevo lectin shows preferential binding towards manno-oligosaccharides with terminal alphaMan(1,2)alphaMan structures, and showed a strong affinity for ManLAM, whereas it binds weakly to Mycobacterium smegmatis (M. smegmatis) lipoarabinomannan (MsmLAM), which displays relatively fewer and shorter mannosyl caps. Crystal structure of Mevo lectin complexed with a Man7D1 revealed the multivalent cross-linking interaction, which explains avidity-based high affinity for these ligands when compared to previously studied manno-oligosaccharides lacking the specific termini. Functional studies suggest that M. tuberculosis internalization by the macrophage was impaired by binding of Mevo lectin to ManLAM present on the surface of M. tuberculosis. Selectivity shown by Mevo lectin towards glycans with terminal alphaMan(1,2)alphaMan structures, and its ability to compromise the internalization of M. tuberculosis in vitro, underscore the potential utility of Mevo lectin as a research tool to study host-pathogen interactions. | ||
| - | + | Mevo lectin specificity towards high-mannose structures with terminal alphaMan(1,2)alphaMan residues and its implication to inhibition of the entry of Mycobacterium tuberculosis into macrophages.,Sivaji N, Harish N, Singh S, Singh A, Vijayan M, Surolia A Glycobiology. 2021 Apr 1. pii: 6207891. doi: 10.1093/glycob/cwab022. PMID:33822039<ref>PMID:33822039</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7ded" style="background-color:#fffaf0;"></div> |
| - | [[Category: Surolia | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Methanococcus voltae A3]] | ||
| + | [[Category: Sivaji N]] | ||
| + | [[Category: Surolia A]] | ||
| + | [[Category: Vijayan M]] | ||
Current revision
Mevo lectin complex with mannoheptose (Man7)
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