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5ajb
From Proteopedia
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<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=5ajb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ajb OCA], [http://pdbe.org/5ajb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ajb RCSB], [http://www.ebi.ac.uk/pdbsum/5ajb PDBsum]</span></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=5ajb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ajb OCA], [http://pdbe.org/5ajb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ajb RCSB], [http://www.ebi.ac.uk/pdbsum/5ajb PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Histo-blood group epitopes are fucosylated branched oligosaccharides with well-defined conformations in solution that are recognized by receptors, such as lectins from pathogens. We report here the results of a series of experimental and computational endeavors revealing the unusual distortion of histo-blood group antigens by bacterial and fungal lectins. The Lewis x trisaccharide adopts a rigid closed conformation in solution, while crystallography and molecular dynamics reveal several higher energy open conformations when bound to the Ralstonia solanacearum lectin, which is in agreement with thermodynamic and kinetic measurements. Extensive molecular dynamics simulations confirm rare transient Lex openings in solution, frequently assisted by distortion of the central N-acetyl-glucosamine ring. Additional directed molecular dynamic trajectories revealed the role of a conserved tryptophan residue in guiding the fucose into the binding site. Our findings show that conformational adaptation of oligosaccharides is of paramount importance in cell recognition and should be considered when designing anti-infective glyco-compounds. | ||
| + | |||
| + | The Hidden Conformation of Lewis x, a Human Histo-Blood Group Antigen, Is a Determinant for Recognition by Pathogen Lectins.,Topin J, Lelimousin M, Arnaud J, Audfray A, Perez S, Varrot A, Imberty A ACS Chem Biol. 2016 May 20. PMID:27198630<ref>PMID:27198630</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5ajb" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:03, 1 June 2016
X-ray structure of the RSL lectin in complex with Lewis X tetrasaccahride
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