3vkl

Protease-resistant mutant form of human Galectin-8 in complex with two lactose molecules

spinqualitylabelsall models 3vkl, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vkl is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BGC, EDO, GAL Related: 4fqz, 3vkm, 3vkn, 3vko Gene: LGALS8 (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [LEG8_HUMAN] Lectin with a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans. Publication Abstract from PubMed Galectin-8 is a tandem-repeat-type beta-galactoside-specific animal lectin having N- and C-terminal carbohydrate recognition domains (N-CRD and C-CRD, respectively) with a difference in carbohydrate-binding specificity, involved in cell-matrix interaction, malignant transformation, and cell adhesion. N-CRD exhibits strong affinity for alpha2-3 sialylated oligosaccharides, a feature unique to galectin-8. C-CRD usually exhibits relatively lower affinity for oligosaccharides, but has higher affinity for N-glycan-type branched oligosaccharides than does N-CRD. There have been many structural studies on galectins with a single CRD, but no X-ray structure of a galectin containing both CRDs has been reported. Here, the X-ray structure of a protease-resistant mutant form of human galectin-8 having both CRDs and the novel pseudo-dimer structure of galectin-8 N-CRD in complexes with alpha2-3 sialylated oligosaccharide ligands were determined. The results revealed a difference in specificity between the N- and C-CRDs, and provided new insights into the association of CRDs and/or molecules of galectin-8. (c) 2012 The Authors Journal compilation (c) 2012 FEBS. X-ray Structure of a Protease-resistant Mutant Form of Human Galectin-8 with Two Carbohydrate Recognition Domains.,Yoshida H, Yamashita S, Teraoka M, Itoh A, Nakakita SI, Nishi N, Kamitori S FEBS J. 2012 Aug 22. doi: 10.1111/j.1742-4658.2012.08753.x. PMID:22913484 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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