1993
DOI: 10.1006/jmbi.1993.1212
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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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Cited by 147 publications
(115 citation statements)
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“…Following the pioneering works of Hardman and Ainsworth (1972) and Edelman et al (1972) on the three-dimensional structure of ConA, the 3D-models of seven lectins have been solved at atomic resolution: PSA from pea (Einspahr et al 1986); Favin from Vicia faba (Reeke & Becker 1986); LoLI from Lathyrus ochrus (Bourne et al 1990a); GSIV from Griffonia simplicifolia (Delbaere et al 1990); EcoL from Erythrina corallodendron (Shaanan et al 1991); PNA from peanut (Banerjee et al 1993) and LCA from lentil (Loris et al 1993). In addition, complexes of legume lectins with simple or more complex sugars were solved by X-ray analysis: ConA with mannose (Derewenda et al 1989); LoLI with glucose and mannose (Bourne et al 1990b), with a trimannoside (Bourne et al 1990c), with an octasaccharide (Bourne et al 1992) of the Nacetyllactosaminic type and with Muramic (MurAc) and N-acetylmuramic (MurNAc) acids (Bourne et al 1994a); PSA with a trimannoside (Rini et al 1993); GSIV with a tetrasaccharide of the Lewis b group (Delbaere et al 1993); LoLII with a glycoprotein (N2) derived from human lactotransferrin (Bourne et al 1994b), and SBA from soybean with a biantennary analog of the blood group I antigen (Dessen et al 1995). These complexes have shown that the monosaccharidebinding site of lectins plays a key role in the binding of either monosaccharides or more complex glycans.…”
mentioning
confidence: 99%
“…Following the pioneering works of Hardman and Ainsworth (1972) and Edelman et al (1972) on the three-dimensional structure of ConA, the 3D-models of seven lectins have been solved at atomic resolution: PSA from pea (Einspahr et al 1986); Favin from Vicia faba (Reeke & Becker 1986); LoLI from Lathyrus ochrus (Bourne et al 1990a); GSIV from Griffonia simplicifolia (Delbaere et al 1990); EcoL from Erythrina corallodendron (Shaanan et al 1991); PNA from peanut (Banerjee et al 1993) and LCA from lentil (Loris et al 1993). In addition, complexes of legume lectins with simple or more complex sugars were solved by X-ray analysis: ConA with mannose (Derewenda et al 1989); LoLI with glucose and mannose (Bourne et al 1990b), with a trimannoside (Bourne et al 1990c), with an octasaccharide (Bourne et al 1992) of the Nacetyllactosaminic type and with Muramic (MurAc) and N-acetylmuramic (MurNAc) acids (Bourne et al 1994a); PSA with a trimannoside (Rini et al 1993); GSIV with a tetrasaccharide of the Lewis b group (Delbaere et al 1993); LoLII with a glycoprotein (N2) derived from human lactotransferrin (Bourne et al 1994b), and SBA from soybean with a biantennary analog of the blood group I antigen (Dessen et al 1995). These complexes have shown that the monosaccharidebinding site of lectins plays a key role in the binding of either monosaccharides or more complex glycans.…”
mentioning
confidence: 99%
“…d-predicted by alignment to ECL. ConA (Naismith et al, 1996), DGL , CFL , OVL (Sharon & Lis, 1990), AHL (Sharma & Surolia, 1997), VFL (Reeke et al, 1986), PSL (Bourne et al, 1990b), UEL-I, II (Sharma & Surolia, 1997), LCL (Sharon & Lis, 1990), LOL (Bourne et al, 1990b), GSL-IV (Delbaere et al, 1993), ECL (Shaanan et al, 1991), DBL (Imberty et al, 1994), GML (Dessan et al, 1995). VML (Calvete et al 1998;Ramos et al 1999) Lectins are designed by initial letter of the plant names.…”
Section: Legume Lectins As Defense Proteinsmentioning
confidence: 99%
“…Furthermore, the co-crystallization of some of these proteins with specific ligands has also given information towards the understanding of the interaction between lectins with simple and complex carbohydrates, revealing which amino acids residues are involved in the interaction between molecular partners. Therefore more properly establishing the monosaccharide bindingsites of these proteins (Bourne et al, 1990b;Shaanan et al, 1991;Delbaere et al, 1993;Naismith et al, 1996). According to their specificity, lectins have been classified as glucose/mannose, Nacetylglucosamine, galactose/Nacetylgalactosamine and fucose-binding specific.…”
Section: Introductionmentioning
confidence: 99%
“…E-mail: larry-murdock@entm.purdue.edu sional structure similarity [3,4]. The tertiary structure is composed of two antiparallel pleated sheets of six and seven strands each that are connected by loops and 13-turns [5]. The majority of plant lectins are secretory proteins that either accumulate in the vacuole or extracellular matrix [2].…”
Section: Introductionmentioning
confidence: 99%
“…Analyses of available legume lectin crystallographic data indicate that, regardless of carbohydrate specificity, the monosaccharide binding sites are very similar and are composed of six residues that interact with the sugars [5][6][7][8][9][10][11]. Included among the legume lectins that have been analyzed are concanavalin A (conA), Lathyrus ochrus isolectin 1 (LOL 1), Griffonia simplicifolia lectin IV (GS-IV), pea lectin, Vicia faba lectin (Favin), phytohemagglutinin (PHA), and Erythrina corallodendron lectin (ECorL).…”
Section: Introductionmentioning
confidence: 99%