3nbd

From Proteopedia

(Difference between revisions)

Current revision

Clitocybe nebularis ricin B-like lectin (CNL) in complex with lactose, crystallized at pH 7.1

Structural highlights

3nbd is a 2 chain structure with sequence from Clitocybe nebularis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.15Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

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^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3nbd"

@@ Line 3: / Line 3: @@
 <StructureSection load='3nbd' size='340' side='right'caption='[[3nbd]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3nbd]] 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=3NBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NBD FirstGlance]. <br>
+<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.15&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3nbc|3nbc]], [[3nbe|3nbe]]</div></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 ==
@@ Line 24: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Cline]]
+[[Category: Clitocybe nebularis]]
 [[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]]

3nbd

From Proteopedia

Current revision

Clitocybe nebularis ricin B-like lectin (CNL) in complex with lactose, crystallized at pH 7.1

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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