-
1
-
-
0031588904
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
12
-
-
0001729674
-
X-ray and molecular dynamics studies of concanavalin-A glucoside and mannoside complexes. Relating structure to thermodynamics of binding
-
Bradbrook GM, Gleichmann T, Harrop SJ, Habash J, Raftery J, Kalb (Gilboa) J, Yariv J, Hillier IH, Helliwell JR X-ray and molecular dynamics studies of concanavalin-A glucoside and mannoside complexes. Relating structure to thermodynamics of binding. J Chem Soc Faraday Trans. 94:1998;1603-1611.
-
(1998)
J Chem Soc Faraday Trans
, vol.94
, pp. 1603-1611
-
-
Bradbrook, G.M.1
Gleichmann, T.2
Harrop, S.J.3
Habash, J.4
Raftery, J.5
Kalb, J.6
Yariv, J.7
Hillier, I.H.8
Helliwell, J.R.9
-
13
-
-
0032586737
-
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
-
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
-
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
-
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
-
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
-
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
-
19
-
-
0031565993
-
Crystal structure of acidic seminal fluid protein (aSFP) at 1.9 Å resolution: A bovine polypeptide of the spermadhesin family
-
Romão MJ, Kölln I, Dias JM, Carvalho AL, Romero A, Varela PF, Sanz L, Töpfer-Petersen E, Calvete JJ Crystal structure of acidic seminal fluid protein (aSFP) at 1.9 Å resolution: a bovine polypeptide of the spermadhesin family. J Mol Biol. 274:1997;650-660.
-
(1997)
J Mol Biol
, vol.274
, pp. 650-660
-
-
Romão, M.J.1
Kölln, I.2
Dias, J.M.3
Carvalho, A.L.4
Romero, A.5
Varela, P.F.6
Sanz, L.7
Töpfer-Petersen, E.8
Calvete, J.J.9
-
20
-
-
0031565824
-
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
-
21
-
-
0032491184
-
Structural basis for the recognition of carbohydrates by human galectin-7
-
Leonidas DD, Vatzaki- EH, Vorum H, Celis JE, Madsen P, Acharya KR Structural basis for the recognition of carbohydrates by human galectin-7. Biochemistry. 37:1998;13930-13940.
-
(1998)
Biochemistry
, vol.37
, pp. 13930-13940
-
-
Leonidas, D.D.1
Vatzaki-, E.H.2
Vorum, H.3
Celis, J.E.4
Madsen, P.5
Acharya, K.R.6
-
22
-
-
0033081409
-
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
-
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
-
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
-
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
-
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
-
27
-
-
0027979382
-
Crystal structure of peanut lectin, a protein with an unusual quaternary structure
-
Banerjee R, Mande SC, Ganesh V, Das K, Dhanaraj V, Mahanta SK, Suguna K, Surolia A, Vijiyan M Crystal structure of peanut lectin, a protein with an unusual quaternary structure. Proc Natl Acad Sci USA. 91:1994;227-231.
-
(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 227-231
-
-
Banerjee, R.1
Mande, S.C.2
Ganesh, V.3
Das, K.4
Dhanaraj, V.5
Mahanta, S.K.6
Suguna, K.7
Surolia, A.8
Vijiyan, M.9
-
28
-
-
0033593246
-
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
-
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
-
30
-
-
0033165986
-
X-ray structure of the native (unligated) mannose-specific bulb lectin from Scilla campanulata (bluebell) at 1.7 Å resolution
-
Wood DD, Wright LM, Reynolds CD, Rizkallah PJ, Allen AK, Peumans WJ, Van Damme EJM X-ray structure of the native (unligated) mannose-specific bulb lectin from Scilla campanulata (bluebell) at 1.7 Å resolution. Acta Crystallogr. D55:1999;1264-1272.
-
(1999)
Acta Crystallogr
, vol.55
, pp. 1264-1272
-
-
Wood, D.D.1
Wright, L.M.2
Reynolds, C.D.3
Rizkallah, P.J.4
Allen, A.K.5
Peumans, W.J.6
Van Damme, E.J.M.7
-
31
-
-
0029658497
-
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
-
32
-
-
0032513154
-
Structure of the complex of Maclura pomifera agglutinin and the T-antigen disaccharide, Galβ1,3GalNAc
-
Lee X, Thompson A, Zhang Z, Ton-That H, Biesterfeld J, Ogata C, Xu L, Johnston R, Young NM Structure of the complex of Maclura pomifera agglutinin and the T-antigen disaccharide, Galβ1,3GalNAc. J Biol Chem. 273:1998;6312-6318.
-
(1998)
J Biol Chem
, vol.273
, pp. 6312-6318
-
-
Lee, X.1
Thompson, A.2
Zhang, Z.3
Ton-That, H.4
Biesterfeld, J.5
Ogata, C.6
Xu, L.7
Johnston, R.8
Young, N.M.9
-
33
-
-
0032951161
-
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
-
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
|