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==Clitocybe nebularis ricin B-like lectin (CNL) in complex with lactose, crystallized at pH 4.4== | |||
<StructureSection load='3nbc' size='340' side='right' caption='[[3nbc]], [[Resolution|resolution]] 1.01Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3nbc]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NBC FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LAT:BETA-LACTOSE'>LAT</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3nbd|3nbd]], [[3nbe|3nbe]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3nbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nbc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nbc RCSB], [http://www.ebi.ac.uk/pdbsum/3nbc PDBsum]</span></td></tr> | |||
</table> | |||
<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> | |||
==See Also== | ==See Also== | ||
*[[Ricin|Ricin]] | *[[Ricin|Ricin]] | ||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cline]] | [[Category: Cline]] | ||
[[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: Clitocybe nebularis ricin b-like lectin]] | ||
[[Category: Lactose]] | [[Category: Lactose]] | ||
[[Category: Sugar binding protein]] | [[Category: Sugar binding protein]] | ||
