View source for 6tig


==Structure of the N terminal domain of Bc2L-C lectin (1-131) in complex with Globo H (H-type 3) antigen==
<StructureSection load='6tig' size='340' side='right'caption='[[6tig]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6tig]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_cenocepacia_J2315 Burkholderia cenocepacia J2315]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TIG 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=NGA:N-ACETYL-D-GALACTOSAMINE'>NGA</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=6tig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tig OCA], [https://pdbe.org/6tig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tig RCSB], [https://www.ebi.ac.uk/pdbsum/6tig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tig ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B4EH86_BURCJ B4EH86_BURCJ] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lectins mediate adhesion of pathogens to host tissues, filling in a key role in the first steps of infection. Belonging to the opportunistic pathogen Burkholderia cenocepacia, BC2L-C is a superlectin with dual carbohydrate specificity, believed to mediate cross-linking between bacteria and host cells. Its C-terminal domain binds to bacterial mannosides while its N-terminal domain (BCL2-CN) recognizes fucosylated human epitopes. BC2L-CN presents a tumor necrosis factor alpha (TNF-) fold previously unseen in lectins with a novel fucose binding mode. We report, here, the production of a novel recombinant form of BC2L-CN (rBC2L-CN2), which allowed better protein stability and unprecedented co-crystallization with oligosaccharides. Isothermal calorimetry measurements showed no detrimental effect on ligand binding and data were obtained on the binding of Globo H hexasaccharide and l-galactose. Crystal structures of rBC2L-CN2 were solved in complex with two blood group antigens: H-type 1 and H-type 3 (Globo H) by X-ray crystallography. They provide new structural information on the binding site, of importance for the structural-based design of glycodrugs as new antimicrobials with antiadhesive properties.

BC2L-C N-Terminal Lectin Domain Complexed with Histo Blood Group Oligosaccharides Provides New Structural Information.,Bermeo R, Bernardi A, Varrot A Molecules. 2020 Jan 7;25(2). pii: molecules25020248. doi:, 10.3390/molecules25020248. PMID:31936166<ref>PMID:31936166</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6tig" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Burkholderia cenocepacia J2315]]
[[Category: Large Structures]]
[[Category: Bermeo R]]
[[Category: Varrot A]]