Structural basis of multivalent galactose‐based dendrimer recognition by human galectin‐7

Ramaswamy, Sneha; Sleiman, Mazen Haj; Masuyer, Geoffrey; Arbez-Gindre, Cécile; Micha-Screttas, Maria; Calogeropoulou, Theodora; Steele, Barry R.; Acharya, K. Ravi

doi:10.1111/febs.13140

Cited by 15 publications

(13 citation statements)

References 82 publications

(115 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The X-ray structure of galectin-7 in complex with synthetic galactose-based dendron with three arms (galectin-7/D2 (4UW5)) was reported (13). In this structure, each galactose-terminus of the three arms of D2 is recognized by one galectin-7 molecule (Fig.…”

Section: N-glycan-type Branched Oligossacharides (17)mentioning

confidence: 99%

“…As Arg239 and Glu258 In galectin-9_N-CRD/LN3 (2ZHM) (16), the bound LN3 has a linear structure which enables GlcNAc −1 to form a hydrogen bond with Asn48. Furthermore, Ala46, which is unique to galectin-9_N-CRD, is proposed to be one of the residues responsible for the high affinity for oligolactosamines (13). This is because an amino acid residue with bulky side chain group at the position of Ala46 (His223 in galectin-9_C-CRD and/or Gln47 in galectin-8_ N-CRD) causes steric hindrance with GlcNAc −1 of LN3.…”

Section: +1mentioning

confidence: 99%

See 1 more Smart Citation

Three-Dimensional Structures of Galectins

Kamitori

2018

TIGG

View full text Add to dashboard Cite

The galectins are a family of β-galactoside-specific animal lectins that contain a conserved carbohydrate recognition domain (CRD) with approximately 140 amino acid residues. There are 14 members in the mammalian galectin family (galectin-1-10, and 11-15), and they have different specificities for oligosaccharides. X-ray structures of the galectin CRD in complexes with oligosaccharides have provided important clues about the oligosaccharide-recognition mechanisms of galectins giving the different specificities. Galectin is divalent in glycan binding due to the association of two CRDs that crosslink with oligosaccharides. The spatial arrangement of the two CRDs is very important for elucidating the biological functions of galectins. Several different spatial arrangements of CRDs are found in X-ray structures of galectins. I herein examined the three-dimensional structures of galectins relevant for biological functions, based on the protein-ligand interactions related with oligosaccharide-specificity, the cross-linking structure by galectin and oligosaccharides, and the spatial arrangements of CRDs. A. IntroductionThe galectins are a family of β-galactoside-specific animal lectins that contain a conserved carbohydrate recognition domain In this review, I examined three-dimensional structures of galectins based on the protein-ligand interactions related with oligosaccharide-specificity, the cross-linking structure by galectin and oligosaccharides, and the spatial arrangements of CRDs of the prototype and tandem-repeat type galectins. 2,7,8,9, 10 stand for human galectin-1, 2, 7, 8, 9, 10, respectively (unless stated otherwise). Figures 2, 3, 4, 5 were drawn with the program PyMOL(23). B. Three-Dimensional Structure of Galectin CRDThe overall structure of galectin-9_C-CRD in complex with LacNAc (galectin-9_C-CRD/LacNAc (PDB ID: 3NV2)) (17) is MINIREVIEW

show abstract

Section: N-glycan-type Branched Oligossacharides (17)mentioning

confidence: 99%

Section: +1mentioning

confidence: 99%

Three-Dimensional Structures of Galectins

Kamitori

2018

TIGG

View full text Add to dashboard Cite

show abstract

“…48 The secondary structure is similar to prototype galectins such as galectin 7 and galectin 10 or Charcot-Leyden crystal protein. 49,50 The C-terminal CRD is of chimera-type galectin (galectin 3). 51 The typical structural alignment of these proteins showed five-stranded (F1-F5) and six-stranded (S1-S6 a/ S6b) b-sheets stabilized by one or two alpha-helices at their ends ( Figure 3).…”

Section: Physical and Chemical Characteristics Of Pp13mentioning

confidence: 99%

“…Experiments done with placental PP13/galectin 13 showed that it contains phosphorylation sites. Computational analysis indicated sites for serine/tyrosine kinase phosphorylation at positioning Ser48 (44)(45)(46)(47)(48)(49)(50)(51)(52)(53)(54)(55)(56)(57) and Tyr41 (37)(38)(39)(40)(41)(42)(43)(44)(45) and Tyr80 (76)(77)(78)(79)(80)(81)(82)(83)(84) close to CRD domain. The carbohydrate binding affinity was observed to be the same in PP13-B (placentally expressed phosphorylated) and PP13-R (bacterially expressed non-phosphorylated).…”

Section: Placental Implantationmentioning

confidence: 99%

Placental protein 13

Gadde

Sheela

2018

Journal of Circulating Biomarkers

View full text Add to dashboard Cite

Placental protein 13 (PP13), a glycan binding protein predominantly expressed in syncytiotrophoblast, dimeric in nature, lacks N-terminal signal peptide, bypasses the endoplasmic reticulum, and secretes into maternal circulation as exosomes or microvesicles. PP13 has jelly roll fold conformation with conserved carbohydrate recognition domain which specifically binds to β-galactosides of the glycan receptors during placentation. PP13 binds to glycosylated receptors on human erythrocytes and brings about hemagglutination by the property of lectin activity; other functions are immunoregulation and vasodilation during placentation and vascularization. The gene LGALS13 located on 19q13.2 comprising four exons expresses a 32-kDa protein with 139 amino acid residues, PP13. Impaired expression due to mutation in the gene leads to a nonfunctional truncated PP13. The low serum levels predict high risk for the onset of preeclampsia or obstetric complications. Hence, PP13 turned to be an early marker for risk assessment of preeclampsia. The recombinant PP13 and monoclonal antibodies availability help for replenishing PP13 in conditions with low serum levels and for detection and prevention of preeclampsia, respectively.

show abstract

“…The substitution at position 74 of an arginine by a serine inhibits the carbohydrates-binding activity of galectin-7 but does not alter the capacity of galectin-7 to form homodimers in solution [ 42 ]. This indicates that binding to oligosaccharides is not required for galectin-7 to form homodimers even if it can slightly modify its conformation and influence the dimers’ stability [ 43 , 44 ]. Regarding carbohydrate binding, galectin-7 displays preferential binding to internal or terminal LacNAc repeat carried by N -glycan ( Figure 1 a) [ 21 , 22 ].…”

Section: Introductionmentioning

confidence: 99%

Galectin-7 in Epithelial Homeostasis and Carcinomas

Advedissian

Deshayes

Viguier

2017

IJMS

View full text Add to dashboard Cite

Galectins are small unglycosylated soluble lectins distributed both inside and outside the cells. They share a conserved domain for the recognition of carbohydrates (CRD). Although galectins have a common affinity for β-galatosides, they exhibit different binding preferences for complex glycans. First described twenty years ago, galectin-7 is a prototypic galectin, with a single CRD, able to form divalent homodimers. This lectin, which is mainly expressed in stratified epithelia, has been described in epithelial tissues as being involved in apoptotic responses, in proliferation and differentiation but also in cell adhesion and migration. Most members of the galectins family have been associated with cancer biology. One of the main functions of galectins in cancer is their immunomodulating potential and anti-angiogenic activity. Indeed, galectin-1 and -3, are already targeted in clinical trials. Another relevant function of galectins in tumour progression is their ability to regulate cell migration and cell adhesion. Among these galectins, galectin-7 is abnormally expressed in various cancers, most prominently in carcinomas, and is involved in cancer progression and metastasis but its precise functions in tumour biology remain poorly understood. In this issue, we will focus on the physiological functions of galectin-7 in epithelia and present the alterations of galectin-7 expression in carcinomas with the aim to describe its possible functions in tumour progression.

show abstract

Structural basis of multivalent galactose‐based dendrimer recognition by human galectin‐7

Cited by 15 publications

References 82 publications

Three-Dimensional Structures of Galectins

Three-Dimensional Structures of Galectins

Placental protein 13

Galectin-7 in Epithelial Homeostasis and Carcinomas

Contact Info

Product

Resources

About