4up4 | pdb_00004up4

Structure of the recombinant lectin PVL from Psathyrella velutina in complex with GlcNAcb-D-1,3Galactoside

spinqualitylabelsall models 4up4, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4up4 is a 2 chain structure with sequence from Lacrymaria velutina. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.95Å Ligands: CA, GAL, NAG, NDG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q309D1_9AGAR Publication Abstract from PubMed Cell surface glycoconjugates present alterations of their structures in chronic diseases and distinct oligosaccharide epitopes have been associated with cancer. Among them, truncated glycans present terminal non-reducing beta-N-acetylglucosamine (GlcNAc) residues that are rare on healthy tissues. Lectins from unconventional sources such as fungi or algi provide novel markers that bind specifically to such epitopes, but their availability may be challenging. A GlcNAc-binding lectin from the fruiting body of the fungus Psathyrella velutina (PVL) has been produced in good yield in bacterial culture. A strong specificity for terminal GlcNAc residues was evidenced by glycan array. Affinity values obtained by microcalorimetry and surface plasmon resonance demonstrated a micromolar affinity for GlcNAcbeta1-3Gal epitopes and for biantennary N-glycans with GlcNAcbeta1-2Man capped branches. Crystal structure of PVL complexed with GlcNAcbeta1-3Gal established the structural basis of the specificity. Labeling of several types of cancer cells and use of inhibitors of glycan metabolism indicated that rPVL binds to terminal GlcNAc but also to sialic acid (Neu5Ac). Analysis of glycosyltransferase expression confirmed the higher amount of GlcNAc present on cancer cells. rPVL binding is specific to cancer tissue and weak or no labeling is observed for healthy ones, except for stomach glands that present unique alphaGlcNAc-presenting mucins. In lung, breast and colon carcinomas, a clear delineation could be observed between cancer regions and surrounding healthy tissues. PVL is therefore a useful tool for labeling agalacto-glycans in cancer or other diseases. A recombinant fungal lectin for labeling truncated glycans on human cancer cells.,Audfray A, Beldjoudi M, Breiman A, Hurbin A, Boos I, Unverzagt C, Bouras M, Lantuejoul S, Coll JL, Varrot A, Le Pendu J, Busser B, Imberty A PLoS One. 2015 Jun 4;10(6):e0128190. doi: 10.1371/journal.pone.0128190., eCollection 2015. PMID:26042789 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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