4pf5: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4pf5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PF5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4pf5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PF5 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=M3N:4-(HYDROXYMETHYL)-1-(ALPHA-D-MANNOPYRANOSYL)-1H-1,2,3-TRIAZOLE'>M3N</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]] 2.04Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=M3N:4-(HYDROXYMETHYL)-1-(ALPHA-D-MANNOPYRANOSYL)-1H-1,2,3-TRIAZOLE'>M3N</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=4pf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pf5 OCA], [https://pdbe.org/4pf5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pf5 RCSB], [https://www.ebi.ac.uk/pdbsum/4pf5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pf5 ProSAT]</span></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=4pf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pf5 OCA], [https://pdbe.org/4pf5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pf5 RCSB], [https://www.ebi.ac.uk/pdbsum/4pf5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pf5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 14:18, 9 May 2024
Structural highlights
FunctionCONA_CANEN D-mannose specific lectin. Publication Abstract from PubMedTerminal "high-mannose oligosaccharides" are involved in a broad range of biological and pathological processes, from sperm-egg fusion to influenza and human immunodeficiency virus infections. In spite of many efforts, their synthesis continues to be very challenging and actually represents a major bottleneck in the field. Whereas multivalent presentation of mannopyranosyl motifs onto a variety of scaffolds has proven to be a successful way to interfere in recognition processes involving high-mannose oligosaccharides, such constructs fail at reproducing the subtle differences in affinity towards the variety of protein receptors (lectins) and antibodies susceptible to binding to the natural ligands. Here we report a family of functional high-mannose oligosaccharide mimics that reproduce not only the terminal mannopyranosyl display, but also the core structure and the branching pattern, by replacing some inner mannopyranosyl units with triazole rings. Such molecular design can be implemented by exploiting "click" ligation strategies, resulting in a substantial reduction of synthetic cost. The binding affinities of the new "click" high-mannose oligosaccharide mimics towards two mannose specific lectins, namely the plant lectin concanavalin A (ConA) and the human macrophage mannose receptor (rhMMR), have been studied by enzyme-linked lectin assays and found to follow identical trends to those observed for the natural oligosaccharide counterparts. Calorimetric determinations against ConA, and X-ray structural data support the conclusion that these compounds are not just another family of multivalent mannosides, but real "structural mimics" of the high-mannose oligosaccharides. Synthesis of High-Mannose Oligosaccharide Analogues through Click Chemistry: True Functional Mimics of Their Natural Counterparts Against Lectins?,Francois-Heude M, Mendez-Ardoy A, Cendret V, Lafite P, Daniellou R, Ortiz Mellet C, Garcia Fernandez JM, Moreau V, Djedaini-Pilard F Chemistry. 2014 Dec 5. doi: 10.1002/chem.201405481. PMID:25483029[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||