6f5w

Photorhabdus asymbiotica lectin (PHL) in complex with propargyl-fucoside

spinqualitylabelsall models 6f5w, resolution 1.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6f5w is a 2 chain structure with sequence from Photorhabdus asymbiotica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.91Å Ligands: CL, DMS, KG1, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C7BLE4_PHOAA Publication Abstract from PubMed Photorhabdus asymbiotica is a gram-negative bacterium that is not only as effective an insect pathogen as other members of the genus, but it also causes serious diseases in humans. The recently identified lectin PHL from P. asymbiotica verifiably modulates an immune response of humans and insects, which supports the idea that the lectin might play an important role in the host-pathogen interaction. Dimeric PHL contains up to seven L-fucose specific binding sites per monomer, and in order to target multiple binding sites of PHL, alpha-L-fucoside-containing di-, tri- and tetravalent glycoclusters were synthesized. Methyl gallate and pentaerythritol were chosen as multivalent scaffolds, and the fucoclusters were built from the above-mentioned cores by coupling with different oligoethylene bridges and propargyl alpha-L-fucosides using 1,3-dipolar azide-alkyne cycloaddition. The interaction between fucoside derivates and PHL was investigated by several biophysical and biological methods, ITC and SPR measurements, hemagglutination inhibition assay and an investigation of bacterial aggregation properties were carried out. Moreover, details of the interaction between PHL and propargyl alpha-L-fucoside as a monomer unit were revealed using X-ray crystallography. Besides this, the interaction with multivalent compounds was studied by NMR techniques. The newly synthesized multivalent fucoclusters proved to be up to several orders of magnitude better ligands than the natural ligand, L-fucose. Title Synthesis of alpha-L-fucopyranoside-presenting glycoclusters and investigation of their interaction with recombinant Photorhabdus asymbiotica lectin (PHL).,Gita J, Herczeg M, Fujdiarova E, Houser J, Kover KE, Borbas A, Wimmerova M, Csavas M Chemistry. 2018 Jan 17. doi: 10.1002/chem.201705853. PMID:29341313 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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