1msa | pdb_00001msa

MANNOSE-SPECIFIC AGGLUTININ (LECTIN) FROM SNOWDROP (GALANTHUS NIVALIS) BULBS COMPLEXED WITH METHYL-ALPHA-D-MANNOSIDE

spinqualitylabelsall models 1msa, resolution 2.29Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1msa is a 4 chain structure with sequence from Galanthus nivalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.29Å Ligands: MMA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LEC_GALNI Mannose-specific lectin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Tetrameric Galanthus nivalis agglutinin (50,000 M(r)) belongs to a super-family of alpha-D-mannose-specific plant bulb lectins known to be potent inhibitors of retroviruses. The 2.3 A crystal structure of this lectin complexed with methyl alpha-D-mannose reveals a novel three-fold symmetric beta-sheet polypeptide fold. Three antiparallel four-stranded beta-sheets, each with a conserved mannose-binding site, are arranged as a 12-stranded beta-barrel. The tetramer displays 222 symmetry. Pairs of monomers form stable dimers through C-terminal strand exchange. The so formed hybrid beta-sheets are the sites for high affinity mannose binding in the dimer interface. Occupancy observed at corresponding sites in other beta-sheets suggests a potential for twelve sites per tetramer. Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family.,Hester G, Kaku H, Goldstein IJ, Wright CS Nat Struct Biol. 1995 Jun;2(6):472-9. PMID:7664110 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Agglutinin 3D structures

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