3nbd
From Proteopedia
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| - | [[Image:3nbd.png|left|200px]] | ||
| - | + | ==Clitocybe nebularis ricin B-like lectin (CNL) in complex with lactose, crystallized at pH 7.1== | |
| + | <StructureSection load='3nbd' size='340' side='right'caption='[[3nbd]], [[Resolution|resolution]] 1.15Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3nbd]] 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=3NBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NBD 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]] 1.15Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900008:alpha-lactose'>PRD_900008</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3nbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nbd OCA], [https://pdbe.org/3nbd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nbd RCSB], [https://www.ebi.ac.uk/pdbsum/3nbd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nbd ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3nbd" style="background-color:#fffaf0;"></div> | |
| - | + | ||
==See Also== | ==See Also== | ||
| - | *[[Ricin|Ricin]] | + | *[[Ricin 3D structures|Ricin 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Clitocybe nebularis]] | [[Category: Clitocybe nebularis]] | ||
| - | [[Category: Kos | + | [[Category: Large Structures]] |
| - | [[Category: Pohleven | + | [[Category: Kos J]] |
| - | [[Category: Renko | + | [[Category: Pohleven J]] |
| - | [[Category: Sabotic | + | [[Category: Renko M]] |
| - | [[Category: Turk | + | [[Category: Sabotic J]] |
| - | + | [[Category: Turk D]] | |
| - | + | ||
| - | + | ||
Current revision
Clitocybe nebularis ricin B-like lectin (CNL) in complex with lactose, crystallized at pH 7.1
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