4i6s

Structure of RSL mutant W76A in complex with L-fucose

spinqualitylabelsall models 4i6s, resolution 1.54Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4i6s is a 3 chain structure with sequence from Ralstonia solanacearum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.54Å Ligands: EDO, FUC, FUL, PG4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D8NA05_RALSL Publication Abstract from PubMed Multivalency is proposed to play a role in the strong avidity of lectins for glycosylated cell surfaces and also in their ability to affect membrane dynamics by clustering glycosphingolipids. Lectins with modified valency were designed from the beta-propeller fold of Ralstonia solanacearum lectin (RSL) that presents six fucose binding sites. After identification of key amino acids by molecular dynamics calculations, two mutants with reduced valency were produced. Isothermal titration calorimetry confirmed the loss of three high affinity binding sites for both mutants. Crystal structures indicated that residual low affinity binding occurred in W76A but not in R17A. The trivalent R17A mutant presented unchanged avidity toward fucosylated surfaces, when compared to hexavalent RSL. However, R17A is not able anymore to induce formation of membrane invaginations on giant unilamellar vesicules, indicating the crucial role of number of binding sites for clustering of glycolipids. In the human lung epithelial cell line H1299, wt-RSL is internalized within seconds whereas the kinetics of R17A uptake is largely delayed. Neolectins with tailored valency are promising tools to study membrane dynamics. Reduction of Lectin Valency Drastically Changes Glycolipid Dynamics in Membranes but Not Surface Avidity.,Arnaud J, Claudinon J, Trondle K, Trovaslet M, Larson G, Thomas A, Varrot A, Romer W, Imberty A, Audfray A ACS Chem Biol. 2013 Jul 23. PMID:23855446 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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