View source for 3qdv


==Structure of the orthorhombic form of the Boletus edulis lectin in complex with N-acetyl glucosamine and N-acetyl galactosamine==
<StructureSection load='3qdv' size='340' side='right'caption='[[3qdv]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3qdv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Boletus_edulis Boletus edulis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QDV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QDV 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]] 1.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</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=3qdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qdv OCA], [https://pdbe.org/3qdv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qdv RCSB], [https://www.ebi.ac.uk/pdbsum/3qdv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qdv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BEL_BOLED BEL_BOLED] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A novel lectin has been isolated from the fruiting bodies of the common edible mushroom Boletus edulis (king bolete, penny bun, porcino, or cep) by affinity chromatography on a chitin column. We propose for the lectin the name BEL (Boletus edulis lectin). BEL inhibits selectively the proliferation of several malignant cell lines and binds the neoplastic cell specific T-antigen disaccharide, Galbeta1-3GalNAc. The lectin was structurally characterized: the molecule is a homotetramer and the 142 amino acid sequence of the chains was determined. The protein belongs to the saline-soluble family of mushroom fruiting body specific lectins. BEL was also crystallized and its three-dimensional structure was determined by X-ray diffraction to 1.15 A resolution. The structure is similar to that of Agaricus bisporus lectin. Using the appropriate co-crystals, the interactions of BEL with specific mono and disaccharides were also studied by X-ray diffraction. The six structures of carbohydrate complexes reported here provide details of the interactions of the ligands with the lectin and shed light on the selectivity of the two distinct binding sites present in each protomer.

STRUCTURE OF A LECTIN WITH ANTITUMORAL PROPERTIES IN KING BOLETE (Boletus edulis) MUSHROOMS.,Bovi M, Carrizo ME, Capaldi S, Perduca M, Chiarelli LR, Galliano M, Monaco HL Glycobiology. 2011 Feb 8. PMID:21303815<ref>PMID:21303815</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3qdv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Boletus edulis]]
[[Category: Large Structures]]
[[Category: Bovi M]]
[[Category: Capaldi S]]
[[Category: Carrizo ME]]
[[Category: Chiarelli LR]]
[[Category: Galliano M]]
[[Category: Monaco HL]]
[[Category: Perduca M]]