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| | <StructureSection load='3nbc' size='340' side='right'caption='[[3nbc]], [[Resolution|resolution]] 1.01Å' scene=''> | | <StructureSection load='3nbc' size='340' side='right'caption='[[3nbc]], [[Resolution|resolution]] 1.01Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3nbc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cline Cline]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NBC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3nbc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clitocybe_nebularis Clitocybe nebularis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NBC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</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]] 1.01Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3nbd|3nbd]], [[3nbe|3nbe]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=PRD_900004:beta-lactose'>PRD_900004</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=3nbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nbc OCA], [https://pdbe.org/3nbc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nbc RCSB], [https://www.ebi.ac.uk/pdbsum/3nbc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nbc 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=3nbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nbc OCA], [https://pdbe.org/3nbc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nbc RCSB], [https://www.ebi.ac.uk/pdbsum/3nbc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nbc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/CNL_CLINE CNL_CLINE] Lectin specific for terminal, non-reducing N-acetylgalactosamine (Gal-NAc)-containing carbohydrates including N,N'-diacetyllactosediamine/LDN (GalNAcbeta1-4GlcNAc, LacdiNAc). Specific also for carbohydrates containing N-acetylglucosamine (-GlcNAc) or N-acetyllactosamine (-Galbeta1-4GlcNAc) at the reducing end. Agglutinates human blood group A, AB, B and O erythrocytes with a strong preference for group A. Agglutinates bovine erythrocytes with a very low specificity (PubMed:19100814, PubMed:22298779). Binds carbohydrates bivalently, which is required for its biological activity (PubMed:22298779). Exhibits insecticidal activity against the fruit fly D.melanogaster, mosquito A.aegypti, and amoebozoa A.castellanii. Has anti-nutritional activity against Colorado potato beetle L.decemlineata, and against worm C.elegans (PubMed:21556921, PubMed:21486374). Has antiproliferative activity against human leukemic T-cells (PubMed:19100814). Has an immunostimulatory effect on human antigen-presenting dendritic cells, which are subsequently able to induce efficient T-cell immune responses (PubMed:22044067).<ref>PMID:19100814</ref> <ref>PMID:21486374</ref> <ref>PMID:21556921</ref> <ref>PMID:22044067</ref> <ref>PMID:22298779</ref> |
| - | Lectins are carbohydrate-binding proteins that exert their biological activity by binding to specific cell glycoreceptors. We have expressed CNL, a ricin B-like lectin from the basidiomycete Clitocybe nebularis, in Escherichia coli. The recombinant lectin, rCNL, agglutinates human blood group A erythrocytes and is specific for the unique glycan N,N'-diacetyllactosediamine (GalNAcbeta1-4GlcNAc, LacdiNAc, LDN) as demonstrated by glycan microarray analysis. We here describe the crystal structures of rCNL in complex with lactose and LDN, defining its interactions with the sugars. CNL is a homodimeric lectin, each of whose monomers comprises a single ricin B lectin domain with its beta-trefoil fold and one carbohydrate-binding site. In order to study the mode of CNL action, a non-sugar-binding mutant and non-dimerizing monovalent mutants that retain carbohydrate-binding activity were prepared. rCNL and the mutants were examined for their biological activities against Jurkat human leukemic T cells and the hypersensitive nematode Caenorhabditis elegans mutant strain pmk-1. rCNL was toxic against both, while the mutants were inactive. Thus, the bivalent carbohydrate-binding property of homodimeric CNL is essential for its activity, providing one of the rare pieces of evidence that certain activities of lectins are associated with their multivalency.
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| - | Bivalent carbohydrate binding is required for biological activity of CNL, the LacdiNAc (GalNAcbeta1-4GlcNAc)-specific lectin from basidiomycete Clitocybe nebularis.,Pohleven J, Renko M, Magister S, Smith DF, Kuenzler M, Strukelj B, Turk D, Kos J, Sabotic J J Biol Chem. 2012 Feb 1. PMID:22298779<ref>PMID:22298779</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div> | + | |
| - | <div class="pdbe-citations 3nbc" style="background-color:#fffaf0;"></div> | + | |
| | | | |
| | ==See Also== | | ==See Also== |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cline]] | + | [[Category: Clitocybe nebularis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kos, J]] | + | [[Category: Kos J]] |
| - | [[Category: Pohleven, J]] | + | [[Category: Pohleven J]] |
| - | [[Category: Renko, M]] | + | [[Category: Renko M]] |
| - | [[Category: Sabotic, J]] | + | [[Category: Sabotic J]] |
| - | [[Category: Turk, D]] | + | [[Category: Turk D]] |
| - | [[Category: Clitocybe nebularis ricin b-like lectin]]
| + | |
| - | [[Category: Lactose]]
| + | |
| - | [[Category: Sugar binding protein]]
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| Structural highlights
Function
CNL_CLINE Lectin specific for terminal, non-reducing N-acetylgalactosamine (Gal-NAc)-containing carbohydrates including N,N'-diacetyllactosediamine/LDN (GalNAcbeta1-4GlcNAc, LacdiNAc). Specific also for carbohydrates containing N-acetylglucosamine (-GlcNAc) or N-acetyllactosamine (-Galbeta1-4GlcNAc) at the reducing end. Agglutinates human blood group A, AB, B and O erythrocytes with a strong preference for group A. Agglutinates bovine erythrocytes with a very low specificity (PubMed:19100814, PubMed:22298779). Binds carbohydrates bivalently, which is required for its biological activity (PubMed:22298779). Exhibits insecticidal activity against the fruit fly D.melanogaster, mosquito A.aegypti, and amoebozoa A.castellanii. Has anti-nutritional activity against Colorado potato beetle L.decemlineata, and against worm C.elegans (PubMed:21556921, PubMed:21486374). Has antiproliferative activity against human leukemic T-cells (PubMed:19100814). Has an immunostimulatory effect on human antigen-presenting dendritic cells, which are subsequently able to induce efficient T-cell immune responses (PubMed:22044067).[1] [2] [3] [4] [5]
See Also
References
- ↑ Pohleven J, Obermajer N, Sabotic J, Anzlovar S, Sepcić K, Kos J, Kralj B, Strukelj B, Brzin J. Purification, characterization and cloning of a ricin B-like lectin from mushroom Clitocybe nebularis with antiproliferative activity against human leukemic T cells. Biochim Biophys Acta. 2009 Mar;1790(3):173-81. PMID:19100814 doi:10.1016/j.bbagen.2008.11.006
- ↑ Bleuler-Martínez S, Butschi A, Garbani M, Wälti MA, Wohlschlager T, Potthoff E, Sabotiĉ J, Pohleven J, Lüthy P, Hengartner MO, Aebi M, Künzler M. A lectin-mediated resistance of higher fungi against predators and parasites. Mol Ecol. 2011 Jul;20(14):3056-70. PMID:21486374 doi:10.1111/j.1365-294X.2011.05093.x
- ↑ Pohleven J, Brzin J, Vrabec L, Leonardi A, Cokl A, Strukelj B, Kos J, Sabotič J. Basidiomycete Clitocybe nebularis is rich in lectins with insecticidal activities. Appl Microbiol Biotechnol. 2011 Aug;91(4):1141-8. PMID:21556921 doi:10.1007/s00253-011-3236-0
- ↑ Svajger U, Pohleven J, Kos J, Strukelj B, Jeras M. CNL, a ricin B-like lectin from mushroom Clitocybe nebularis, induces maturation and activation of dendritic cells via the toll-like receptor 4 pathway. Immunology. 2011 Dec;134(4):409-18. PMID:22044067 doi:10.1111/j.1365-2567.2011.03500.x
- ↑ Pohleven J, Renko M, Magister S, Smith DF, Kuenzler M, Strukelj B, Turk D, Kos J, Sabotic J. Bivalent carbohydrate binding is required for biological activity of CNL, the LacdiNAc (GalNAcbeta1-4GlcNAc)-specific lectin from basidiomycete Clitocybe nebularis. J Biol Chem. 2012 Feb 1. PMID:22298779 doi:10.1074/jbc.M111.317263
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