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The authors demonstrate that half the subunits in two lectins from Dolichos biflorus have an additional helix at their C terminus that is involved in quaternary interactions and the generation of adenine-binding sites.
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Carbohydrate specificity and quaternary association in basic winged bean lectin: X-ray analysis of the lectin at 2.5 Å
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The structure described provides convincing evidence that variability in quaternary association in legume lectins is caused by factors that are intrinsic to the protein.
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Prabu M.M., Sankaranarayanan R., Puri K.D., Sharma V., Surolia A., Vijayan M., Suguna K. Carbohydrate specificity and quaternary association in basic winged bean lectin: X-ray analysis of the lectin at 2.5 Å J Mol Biol. 276:1998;787-796. The structure described provides convincing evidence that variability in quaternary association in legume lectins is caused by factors that are intrinsic to the protein.
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Crystal structure of the arcelin-1 dimer from Phaseolus vulgaris at 1.9 Å resolution
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0032513154
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Structure of the complex of Maclura pomifera agglutinin and the T antigen disaccharide, Gal-β-1,3GalNAc
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Lee X., Thompson A., Zhang Z., Ton-that H., Biesterfeldt J., Ogata C., Xu L., Johnston R.A., Young N.M. Structure of the complex of Maclura pomifera agglutinin and the T antigen disaccharide, Gal-β-1,3GalNAc. J Biol Chem. 273:1998;6312-6318.
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The authors describe the first dimeric bulb lectin to be structurally characterised. The structure demonstrates the possibility of oligomerisation as a strategy for generating carbohydrate specificity.
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Chandra N.R., Ramachandraiah G., Bachhawat K., Dam T.K., Surolia A., Vijayan M. Crystal structure of a dimeric mannose-specific agglutinin from garlic: quaternary association and carbohydrate specificity. J Mol Biol. 285:1999;1157-1168. The authors describe the first dimeric bulb lectin to be structurally characterised. The structure demonstrates the possibility of oligomerisation as a strategy for generating carbohydrate specificity.
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Chandra, N.R.1
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Vijayan, M.6
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0033516704
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Insights into carbohydrate recognition by Narcissus pseudonarcissus lectin. The crystal structure at 2 Å resolution in complex with β-1,3-mannobiose
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Sauerborn M.K., Wright L.M., Reynolds C.D., Grossman J.G., Rizkallah P.J. Insights into carbohydrate recognition by Narcissus pseudonarcissus lectin. The crystal structure at 2 Å resolution in complex with β-1,3-mannobiose. J Mol Biol. 290:1999;185-199.
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27
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0033165986
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Structure of the native (unligated) mannose-specific bulb lectin from Scilla campanulata (bluebell) at 1.7 Å resolution
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Wood S.D., Wright L.M., Reynolds C.D., Rizkallah P.J., Allen A.K., Peumans W.J., Van Damme E.J.M. Structure of the native (unligated) mannose-specific bulb lectin from Scilla campanulata (bluebell) at 1.7 Å resolution. Acta Crystallogr. D55:1999;1264-1272.
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28
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0032536859
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Crystal structure of the angiogenesis inhibitor endostatin at 1.5 Å resolution
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Structure of the cell-adhesion fragment of intimin from enteropathogenic Escherichia coli
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This paper provides the first atomic resolution structural insight into the basis of E. coli-host cell interactions, important in cell adhesion, mediated through its C-type lectin-like domain of the protein intimin.
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Kelly G., Prasannan S., Daniell S., Fleming K., Frankel G., Dougan G., Connerton I., Matthews S. Structure of the cell-adhesion fragment of intimin from enteropathogenic Escherichia coli. Nat Struct Biol. 6:1999;313-318. This paper provides the first atomic resolution structural insight into the basis of E. coli-host cell interactions, important in cell adhesion, mediated through its C-type lectin-like domain of the protein intimin.
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Kelly, G.1
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Frankel, G.5
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Matthews, S.8
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0033053772
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Structure of CD94 reveals a novel C-type lectin fold: Implications for the NK cell-associated CD94/NKG2 receptors
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Boyington J.C., Riaz A.N., Patamawenu A., Coligan J.E., Brooks A.G., Sun P.D. Structure of CD94 reveals a novel C-type lectin fold: implications for the NK cell-associated CD94/NKG2 receptors. Immunity. 10:1999;75-82.
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Boyington, J.C.1
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Sun, P.D.6
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31
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0032167622
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Structure of the C type lectin carbohydrate recognition domain of human tetranectin
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Kastrup J.S., Nielsen B.B., Rasmussen H., Holtet T.L., Graversen J.H., Etzerodt M., Thogersen H.C., Larsen I.K. Structure of the C type lectin carbohydrate recognition domain of human tetranectin. Acta Crystallogr D54:757-766. 1998.
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Larsen, I.K.8
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32
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0032492659
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The solution structure of type-II antifreeze protein reveals a new member of the lectin family
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Gromwald W., Loewen M.C., Lix B., Daugulis A.J., Sonnichsen F.D., Davies P.L., Sykes B.D. The solution structure of type-II antifreeze protein reveals a new member of the lectin family. Biochemistry. 37:1998;4712-4721.
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Gromwald, W.1
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Davies, P.L.6
Sykes, B.D.7
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0033103527
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Crystal structure of the trimeric β-helical coiled-coil and the three lectin domains of human lung surfactant protein D
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Hakansson K., Lim N.K., Hoppe H.-J., Reid B.M. Crystal structure of the trimeric β-helical coiled-coil and the three lectin domains of human lung surfactant protein D. Structure. 7:1999;255-264.
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Hakansson, K.1
Lim, N.K.2
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Reid, B.M.4
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0032037915
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Crystal structure of the N-terminal domain of sialoadhesin in complex with 3′ sialyllactose at 1.85 Å resolution
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The structure determination provides the first example of an I-lectin fold, which is a variant of the V-set immunoglobulin-like fold. The variations appear to be important in adapting the V-set fold to sialic-acid-mediated recognition.
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May A.P., Robinson R.C., Vinson M., Crocker P.R., Jones E.Y. Crystal structure of the N-terminal domain of sialoadhesin in complex with 3′ sialyllactose at 1.85 Å resolution. Mol Cell. 1:1998;719-728. The structure determination provides the first example of an I-lectin fold, which is a variant of the V-set immunoglobulin-like fold. The variations appear to be important in adapting the V-set fold to sialic-acid-mediated recognition.
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May, A.P.1
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Jones, E.Y.5
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35
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0032524316
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Molecular basis of lysosomal enzyme recognition: Three dimensional structure of the cation-dependent mannose 6-phosphate receptor
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The structure determination provides the first example of a P-lectin fold. The fold consists of a nine-stranded flattened β barrel. The distance between the two ligand-binding sites of the dimer provides a structural basis for the differences in binding affinity towards various lysosomal enzymes.
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Roberts D.L., Weix D.J., Dahms N.M., Kim J.-J.P. Molecular basis of lysosomal enzyme recognition: three dimensional structure of the cation-dependent mannose 6-phosphate receptor. Cell. 93:1998;639-648. The structure determination provides the first example of a P-lectin fold. The fold consists of a nine-stranded flattened β barrel. The distance between the two ligand-binding sites of the dimer provides a structural basis for the differences in binding affinity towards various lysosomal enzymes.
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Roberts, D.L.1
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0033522446
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Tachylectin-2: Crystal structure of a specific GlcNAc/GalNAc-binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus
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The structure of tachylectin-2 reveals a new fivefold symmetric lectin fold displaying a five-bladed β-propeller structure. It exhibits five virtually identical binding sites, each associated with a w-like module of the lectin, with high specificity for N-acetylglucosamine. The high number of binding sites within the single polypeptide chain strongly suggests the recognition of carbohydrate surface structures of pathogens with a fairly high ligand density.
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Beisel H.-G., Kawabata S.-I., Iwanaga S., Huber R., Bode W. Tachylectin-2: crystal structure of a specific GlcNAc/GalNAc-binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus. EMBO J. 18:1999;2313-2322. The structure of tachylectin-2 reveals a new fivefold symmetric lectin fold displaying a five-bladed β-propeller structure. It exhibits five virtually identical binding sites, each associated with a w-like module of the lectin, with high specificity for N-acetylglucosamine. The high number of binding sites within the single polypeptide chain strongly suggests the recognition of carbohydrate surface structures of pathogens with a fairly high ligand density.
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EMBO J
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Beisel, H.-G.1
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37
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0033120809
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Variability in quaternary association of proteins with the same tertiary fold: A case study and rationalization involving legume lectins
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This paper presents a comprehensive discussion of the quaternary structures observed in legume lectins and their rationalisation in terms of buried hydrophobic surface area, shape complementarity and interaction energy.
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Prabu M.M., Suguna K., Vijayan M. Variability in quaternary association of proteins with the same tertiary fold: a case study and rationalization involving legume lectins. Proteins. 35:1999;58-69. This paper presents a comprehensive discussion of the quaternary structures observed in legume lectins and their rationalisation in terms of buried hydrophobic surface area, shape complementarity and interaction energy.
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Analysis of hydrophobicity in the alpha and beta chemokine families and its relevance to dimerization
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Molecular recognition of a human blood group determinant by a plant lectin
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Delbaere L.T.J., Vandonselaar M., Prasad L., Quail J.W., Pearlstone J.W., Carpenter M.R., Smillie L.B., Nikrad P.V., Spohr U., Lemieux R.U. Molecular recognition of a human blood group determinant by a plant lectin. Can J Chem. 215:1990;571-584.
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Smillie, L.B.7
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0027196879
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Structure of the lectin IV of Griffonia simplicifolia and its complex with the Lewis b human blood group determinant at 2.0 Å resolution
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