메뉴 건너뛰기




Volumn 9, Issue 5, 1999, Pages 572-577

Novel structures of plant lectins and their complexes with carbohydrates

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE; CARBOHYDRATE; JACALIN; LECTIN; PHYTOHORMONE; PLANT LECTIN;

EID: 0032872116     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(99)00007-X     Document Type: Review
Times cited : (70)

References (34)
  • 1
    • 0031588904 scopus 로고    scopus 로고
    • Analyses of carbohydrate recognition by legume lectins: Size of the combining site loops and their primary specificity
    • Sharma V, Surolia A Analyses of carbohydrate recognition by legume lectins: size of the combining site loops and their primary specificity. J Mol Biol. 267:1997;433-445.
    • (1997) J Mol Biol , vol.267 , pp. 433-445
    • Sharma, V.1    Surolia, A.2
  • 2
    • 0033525658 scopus 로고    scopus 로고
    • Carbohydrate binding, a novel quaternary structure and a novel hydrophobic binding site in two legume lectin oligomers from Dolichos biflorus
    • The crystal structures of two related lectins from Dolichos biflorus (DB58 and DBL) are presented. The two carbohydrate complexes, combined with mutagenesis studies, explain in detail the carbohydrate specificity of this lectin. DBL and DB58 exhibit novel and surprising quaternary structures involving an α helix sandwiched between two β sheets. This unusual interface hosts the binding site for adenine and plant hormones.
    • Hamelryck TW, Loris R, Bouckaert J, Dao-Thi M-H, Strecker G, Imberty A, Fernandez E, Wyns L, Etzler ME Carbohydrate binding, a novel quaternary structure and a novel hydrophobic binding site in two legume lectin oligomers from Dolichos biflorus. J Mol Biol. 286:1999;1161-1177. The crystal structures of two related lectins from Dolichos biflorus (DB58 and DBL) are presented. The two carbohydrate complexes, combined with mutagenesis studies, explain in detail the carbohydrate specificity of this lectin. DBL and DB58 exhibit novel and surprising quaternary structures involving an α helix sandwiched between two β sheets. This unusual interface hosts the binding site for adenine and plant hormones.
    • (1999) J Mol Biol , vol.286 , pp. 1161-1177
    • Hamelryck, T.W.1    Loris, R.2    Bouckaert, J.3    Dao-Thi, M.-H.4    Strecker, G.5    Imberty, A.6    Fernandez, E.7    Wyns, L.8    Etzler, M.E.9
  • 3
    • 0030015445 scopus 로고    scopus 로고
    • Mutational studies of the amino acid residues in the combining site of Erythrina corallodendron lectin
    • Adar R, Sharon N Mutational studies of the amino acid residues in the combining site of Erythrina corallodendron lectin. Eur J Biochem. 239:1996;668-674.
    • (1996) Eur J Biochem , vol.239 , pp. 668-674
    • Adar, R.1    Sharon, N.2
  • 4
    • 0031051545 scopus 로고    scopus 로고
    • Studies by site-directed mutagenesis of the carbohydrate-binding properties of a bark lectin from Robinia pseudoacacia
    • Nishiguchi M, Yoshida K, Sumizono T, Tazaki K Studies by site-directed mutagenesis of the carbohydrate-binding properties of a bark lectin from Robinia pseudoacacia. FEBS Lett. 403:1997;294-298.
    • (1997) FEBS Lett , vol.403 , pp. 294-298
    • Nishiguchi, M.1    Yoshida, K.2    Sumizono, T.3    Tazaki, K.4
  • 5
    • 0033522446 scopus 로고    scopus 로고
    • 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
    • Not a plant lectin, but, nevertheless, a very interesting structure introducing a novel fold and nicely illustrating that the basic principles behind carbohydrate recognition are similar for animal and plant lectins.
    • 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. Not a plant lectin, but, nevertheless, a very interesting structure introducing a novel fold and nicely illustrating that the basic principles behind carbohydrate recognition are similar for animal and plant lectins.
    • (1999) EMBO J , vol.18 , pp. 2313-2322
    • Beisel, H.-G.1    Kawabata, S.-I.2    Iwanaga, S.3    Huber, R.4    Bode, W.5
  • 6
    • 0032502896 scopus 로고    scopus 로고
    • Structures of the Erythrina corallodendron lectin and of its complexes with mono- And disaccharides
    • Elgavish S, Shaanan B Structures of the Erythrina corallodendron lectin and of its complexes with mono- and disaccharides. J Mol Biol. 277:1998;917-932.
    • (1998) J Mol Biol , vol.277 , pp. 917-932
    • Elgavish, S.1    Shaanan, B.2
  • 7
    • 0031719924 scopus 로고    scopus 로고
    • Molecular basis of recognition by Gal/GalNAc specific legume lectins: Influence of Glu129 on the specificity of peanut agglutinin (PNA) towards C2-substituents of galactose
    • Sharma V, Srinivas VR, Adhikari P, Vijayan M, Surolia A Molecular basis of recognition by Gal/GalNAc specific legume lectins: influence of Glu129 on the specificity of peanut agglutinin (PNA) towards C2-substituents of galactose. Glycobiology. 8:1998;1007-1012.
    • (1998) Glycobiology , vol.8 , pp. 1007-1012
    • Sharma, V.1    Srinivas, V.R.2    Adhikari, P.3    Vijayan, M.4    Surolia, A.5
  • 8
    • 0032489360 scopus 로고    scopus 로고
    • Carbohydrate specificity and quaternary association in basic winged bean lectin: X-ray analysis of the lectin at 2.5 Å resolution
    • Prabu MM, Sankaranarayanan R, Puri KD, 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 resolution. J Mol Biol. 276:1998;787-796.
    • (1998) J Mol Biol , vol.276 , pp. 787-796
    • Prabu, M.M.1    Sankaranarayanan, R.2    Puri, K.D.3    Sharma, V.4    Surolia, A.5    Vijayan, M.6    Suguna, K.7
  • 9
    • 0027985523 scopus 로고
    • Molecular modeling of the Dolichos biflorus seed lectin and its specific interactions with carbohydrates: Α-D-N-acetyl-galactosamine, Forssman disaccharide and blood group A trisaccharide
    • Imberty A, Casset F, Gegg CV, Etzler ME, Pérez S Molecular modeling of the Dolichos biflorus seed lectin and its specific interactions with carbohydrates: α-D-N-acetyl-galactosamine, Forssman disaccharide and blood group A trisaccharide. Glycoconjugate J. 11:1994;400-413.
    • (1994) Glycoconjugate J , vol.11 , pp. 400-413
    • Imberty, A.1    Casset, F.2    Gegg, C.V.3    Etzler, M.E.4    Pérez, S.5
  • 10
    • 0031047290 scopus 로고    scopus 로고
    • Transferred NOEs and ROEs reflect the size of the bound segment of the Forssman pentasaccharide in the binding site of Dolichos biflorus lectin
    • Casset F, Imberty A, Pérez S, Etzler ME, Paulsen H, Peters T Transferred NOEs and ROEs reflect the size of the bound segment of the Forssman pentasaccharide in the binding site of Dolichos biflorus lectin. Eur J Biochem. 244:1997;242-250.
    • (1997) Eur J Biochem , vol.244 , pp. 242-250
    • Casset, F.1    Imberty, A.2    Pérez, S.3    Etzler, M.E.4    Paulsen, H.5    Peters, T.6
  • 11
    • 0032878247 scopus 로고    scopus 로고
    • The crystal structures of Man(α1-3)Man(α1-O)Me and Man(α1-6)Man(α1-O)Me in complex with concanavalin A
    • in press. The crystal structures of concanavalin A complexed with Man(α1-3)Man(α1-O)Me and Man(α1-6)Man(α1-O)Me are discussed in view of recently published thermodynamic data. The large change in heat capacity upon binding Man(α1-3)Man(α1-O)Me agrees well with the binding of the reducing mannose to a hydrophobic surface
    • Bouckaert J, Hamelryck T, Wyns L, Loris R: The crystal structures of Man(α1-3)Man(α1-O)Me and Man(α1-6)Man(α1-O)Me in complex with concanavalin A. J Biol Chem 1999, in press. The crystal structures of concanavalin A complexed with Man(α1-3)Man(α1-O)Me and Man(α1-6)Man(α1-O)Me are discussed in view of recently published thermodynamic data. The large change in heat capacity upon binding Man(α1-3)Man(α1-O)Me agrees well with the binding of the reducing mannose to a hydrophobic surface.
    • (1999) J Biol Chem
    • Bouckaert, J.1    Hamelryck, T.2    Wyns, L.3    Loris, R.4
  • 13
    • 0032586737 scopus 로고    scopus 로고
    • Man α1-2 Man α-OMe-concanavalin A complex reveals a balance of forces involved in carbohydrate recognition
    • Moothoo DN, Canan B, Field RA, Naismith JH Man α1-2 Man α-OMe-concanavalin A complex reveals a balance of forces involved in carbohydrate recognition. Glycobiology. 9:1999;539-545.
    • (1999) Glycobiology , vol.9 , pp. 539-545
    • Moothoo, D.N.1    Canan, B.2    Field, R.A.3    Naismith, J.H.4
  • 14
    • 0031934283 scopus 로고    scopus 로고
    • Concanavalin A distorts the β-GlcNAc (12)-Man linkage of α-GlcNac-(1→2)-α-Man-(1→3)-[β-GlcNac-(1→2)- α-Man-(1→6)]-Man upon binding
    • The oligosaccharide that binds most tightly to concanavalin A adopts a conformation in which one of its glycosidic linkages is significantly distorted from its theoretical energetic minimum. This structure provides one of the rare examples for which the bound conformation of an oligosaccharide does not correspond to one of the dominant conformations present in solution.
    • Moothoo DN, Naismith JH Concanavalin A distorts the β-GlcNAc (12)-Man linkage of α-GlcNac-(1→2)-α-Man-(1→3)-[β-GlcNac-(1→2)- α-Man-(1→6)]-Man upon binding. Glycobiology. 8:1998;173-181. The oligosaccharide that binds most tightly to concanavalin A adopts a conformation in which one of its glycosidic linkages is significantly distorted from its theoretical energetic minimum. This structure provides one of the rare examples for which the bound conformation of an oligosaccharide does not correspond to one of the dominant conformations present in solution.
    • (1998) Glycobiology , vol.8 , pp. 173-181
    • Moothoo, D.N.1    Naismith, J.H.2
  • 15
    • 0032484210 scopus 로고    scopus 로고
    • Crystal structure of the lectin from Dioclea grandiflora complexed with core trimannoside of asparagine-linked carbohydrates
    • Rozwarski DA, Swami BM, Brewer CF, Sacchettini JC Crystal structure of the lectin from Dioclea grandiflora complexed with core trimannoside of asparagine-linked carbohydrates. J Biol Chem. 273:1998;32818-21825.
    • (1998) J Biol Chem , vol.273 , pp. 32818-21825
    • Rozwarski, D.A.1    Swami, B.M.2    Brewer, C.F.3    Sacchettini, J.C.4
  • 16
    • 0032168644 scopus 로고    scopus 로고
    • The quaternary structure of UEA-II, the chitobiose specific lectin from gorse
    • Dao-Thi M-H, Rizkallah P, Wyns L, Poortmans F, Loris R The quaternary structure of UEA-II, the chitobiose specific lectin from gorse. Acta Crystallogr. D54:1998;844-847.
    • (1998) Acta Crystallogr , vol.54 , pp. 844-847
    • Dao-Thi, M.-H.1    Rizkallah, P.2    Wyns, L.3    Poortmans, F.4    Loris, R.5
  • 17
    • 0032567433 scopus 로고    scopus 로고
    • x oligosaccharide, an oncofetal antigen
    • This first detailed structural characterization of a type-II two-dimensional cross-link provides a better model for the cross-linking processes that occur at cell surfaces than the better studied three-dimensional cross-links.
    • x oligosaccharide, an oncofetal antigen. J Biol Chem. 273:1998;35016-35022. This first detailed structural characterization of a type-II two-dimensional cross-link provides a better model for the cross-linking processes that occur at cell surfaces than the better studied three-dimensional cross-links.
    • (1998) J Biol Chem , vol.273 , pp. 35016-35022
    • Cheng, W.1    Bullit, E.2    Bhattacharyya, L.3    Brewer, C.F.4    Makowski, L.5
  • 18
    • 0033120809 scopus 로고    scopus 로고
    • Variability in quaternary association of proteins with the same tertiary fold: A case study and rationalization involving legume lectins
    • Prabu MM, 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.
    • (1999) Proteins , vol.35 , pp. 58-69
    • Prabu, M.M.1    Suguna, K.2    Vijayan, M.3
  • 20
    • 0031565824 scopus 로고    scopus 로고
    • The 2.4 Å resolution crystal structure of boar seminal plasma PSP-I/PSP-II: A zona pellucida-binding glycoprotein heterodimer of the spermadhesin family built by a CUB domain architecture
    • Varela PF, Romero A, Sanz L, Romão MJ, Töpfer-Petersen E, Calvete JJ The 2.4 Å resolution crystal structure of boar seminal plasma PSP-I/PSP-II: a zona pellucida-binding glycoprotein heterodimer of the spermadhesin family built by a CUB domain architecture. J Mol Biol. 274:1997;635-649.
    • (1997) J Mol Biol , vol.274 , pp. 635-649
    • Varela, P.F.1    Romero, A.2    Sanz, L.3    Romão, M.J.4    Töpfer-Petersen, E.5    Calvete, J.J.6
  • 22
    • 0033081409 scopus 로고    scopus 로고
    • The physiological structure of human C-reactive protein and its complex with phosphocholine
    • Thompson D, Pepys MB, Wood SP The physiological structure of human C-reactive protein and its complex with phosphocholine. Structure. 7:1999;169-177.
    • (1999) Structure , vol.7 , pp. 169-177
    • Thompson, D.1    Pepys, M.B.2    Wood, S.P.3
  • 23
    • 0029064070 scopus 로고
    • Multiplicity of lectin-carbohydrate interactions
    • Drickamer K Multiplicity of lectin-carbohydrate interactions. Nat Struct Biol. 2:1995;437-439.
    • (1995) Nat Struct Biol , vol.2 , pp. 437-439
    • Drickamer, K.1
  • 24
    • 0001484582 scopus 로고    scopus 로고
    • Multivalent lectin-carbohydrate cross-linking interactions
    • Brewer CF Multivalent lectin-carbohydrate cross-linking interactions. Chemtracts Biochem Mol Biol. 6:1996;165-179.
    • (1996) Chemtracts Biochem Mol Biol , vol.6 , pp. 165-179
    • Brewer, C.F.1
  • 25
    • 0027754166 scopus 로고
    • X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9 Å resolution
    • Lobsanov YD, Gitt MA, Leffler H, Barondes SH, Rini JM X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9 Å resolution. J Biol Chem. 268:1993;27034-27038.
    • (1993) J Biol Chem , vol.268 , pp. 27034-27038
    • Lobsanov, Y.D.1    Gitt, M.A.2    Leffler, H.3    Barondes, S.H.4    Rini, J.M.5
  • 26
    • 0027958144 scopus 로고
    • Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein
    • Liao D-I, Kapadia G, Ahmed H, Vasta GR, Herzberg O Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein. Proc Natl Acad Sci USA. 91:1994;1428-1432.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1428-1432
    • Liao, D.-I.1    Kapadia, G.2    Ahmed, H.3    Vasta, G.R.4    Herzberg, O.5
  • 28
    • 0033593246 scopus 로고    scopus 로고
    • Crystal structure of a dimeric mannose-specific agglutinin from garlic: Quaternary association and carbohydrate specificity
    • This detailed structural analysis of a dimeric monocot lectin indicates its quaternary structure as a major determinant of the different oligosaccharide specificities between heterodimeric garlic lectin and homotetrameric snowdrop lectin. The A subunit of this lectin contains four, rather than the expected three, saccharide-binding sites.
    • Chandra NR, Ramachandraiah G, Bachhawat K, Dam TK, 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. This detailed structural analysis of a dimeric monocot lectin indicates its quaternary structure as a major determinant of the different oligosaccharide specificities between heterodimeric garlic lectin and homotetrameric snowdrop lectin. The A subunit of this lectin contains four, rather than the expected three, saccharide-binding sites.
    • (1999) J Mol Biol , vol.285 , pp. 1157-1168
    • Chandra, N.R.1    Ramachandraiah, G.2    Bachhawat, K.3    Dam, T.K.4    Surolia, A.5    Vijayan, M.6
  • 29
    • 0033516704 scopus 로고    scopus 로고
    • Insights into carbohydrate recognition by Narcissus pseudonarcissus lectin: The crystal structure at 2 Å resolution in complex with α1→3-mannobiose
    • Four disaccharide-binding sites are observed for each monomer of this apparently tetrameric lectin. The unique fourth site is located near the pseudo-threefold axis of the daffodil lectin monomer and may explain the high affinity of this lectin for complex hybrid oligomannose glycans.
    • Sauerborn MK, Wright LM, Reynolds CD, Grossmann JG, Rizkallah PJ Insights into carbohydrate recognition by Narcissus pseudonarcissus lectin: the crystal structure at 2 Å resolution in complex with α1→3-mannobiose. J Mol Biol. 290:1999;185-199. Four disaccharide-binding sites are observed for each monomer of this apparently tetrameric lectin. The unique fourth site is located near the pseudo-threefold axis of the daffodil lectin monomer and may explain the high affinity of this lectin for complex hybrid oligomannose glycans.
    • (1999) J Mol Biol , vol.290 , pp. 185-199
    • Sauerborn, M.K.1    Wright, L.M.2    Reynolds, C.D.3    Grossmann, J.G.4    Rizkallah, P.J.5
  • 31
    • 0029658497 scopus 로고    scopus 로고
    • The 2.0 Å structure of a cross-linked complex between snowdrop lectin and a branched mannopentaose: Evidence for two unique binding modes
    • Wright CS, Hester G The 2.0 Å structure of a cross-linked complex between snowdrop lectin and a branched mannopentaose: evidence for two unique binding modes. Structure. 4:1996;1339-1352.
    • (1996) Structure , vol.4 , pp. 1339-1352
    • Wright, C.S.1    Hester, G.2
  • 33
    • 0032951161 scopus 로고    scopus 로고
    • KM+, a mannose-binding lectin from Artocarpus integrifolia: Amino acid sequence, predicted tertiary structure, carbohydrate recognition, and analysis of the β-prism fold
    • The first report to explain mannose and galactose discrimination in the jacalin family. An analysis is also given of conserved structural determinants of the β-prism fold.
    • Rosa JC, Lopes De Oliveira PS, Garratt R, Beltramini LB, Resing K, Roque-Barreira M-C, Greene LJ KM+, a mannose-binding lectin from Artocarpus integrifolia: amino acid sequence, predicted tertiary structure, carbohydrate recognition, and analysis of the β-prism fold. Protein Sci. 8:1999;13-24. The first report to explain mannose and galactose discrimination in the jacalin family. An analysis is also given of conserved structural determinants of the β-prism fold.
    • (1999) Protein Sci , vol.8 , pp. 13-24
    • Rosa, J.C.1    Lopes De Oliveira, P.S.2    Garratt, R.3    Beltramini, L.B.4    Resing, K.5    Roque-Barreira, M.-C.6    Greene, L.J.7
  • 34
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of Molscript that includes greatly enhanced coloring capabilities
    • Esnouf RM An extensively modified version of Molscript that includes greatly enhanced coloring capabilities. J Mol Graph Model. 15:1997;132-143.
    • (1997) J Mol Graph Model , vol.15 , pp. 132-143
    • Esnouf, R.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.