Relevant bibliographies by topics / Beta-prism I fold lectins

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Academic literature on the topic 'Beta-prism I fold lectins'

Author: Grafiati
Published: 6 September 2023

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Journal articles on the topic "Beta-prism I fold lectins"

1

Sivaji, N., K. V. Abhinav, and M. Vijayan. "Crystallization and biochemical characterization of an archaeal lectin fromMethanococcus voltaeA3." Acta Crystallographica Section F Structural Biology Communications 73, no. 5 (2017): 300–304. http://dx.doi.org/10.1107/s2053230x17006173.

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A lectin fromMethanococcus voltaeA3 has been cloned, expressed, purified and characterized. The lectin appears to be specific for complex sugars. The protein crystallized in a tetragonal space group, with around 16 subunits in the asymmetric unit. Sequence comparisons indicate the lectin to have a β-prism I fold, with poor homology to lectins of known three-dimensional structure.
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2

Ogawa, Tomohisa, Rie Sato, Takako Naganuma, et al. "Diversified Biomineralization Roles of Pteria penguin Pearl Shell Lectins as Matrix Proteins." International Journal of Molecular Sciences 22, no. 3 (2021): 1081. http://dx.doi.org/10.3390/ijms22031081.

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Previously, we isolated jacalin-related lectins termed PPL2, PPL3 (PPL3A, 3B and 3C) and PPL4 from the mantle secretory fluid of Pteria penguin (Mabe) pearl shell. They showed the sequence homology with the plant lectin family, jacalin-related β-prism fold lectins (JRLs). While PPL3s and PPL4 shared only 35%–50% homology to PPL2A, respectively, they exhibited unique carbohydrate binding properties based on the multiple glycan-binding profiling data sets from frontal affinity chromatography analysis. In this paper, we investigated biomineralization properties of these lectins and compared their biomineral functions. It was found that these lectins showed different effects on CaCO3 crystalization, respectively, although PPL3 and PPL2A showed similar carbohydrate binding specificities. PPL3 suppressed the crystal growth of CaCO3 calcite, while PPL2A increased the number of contact polycrystalline calcite composed of more than one crystal with various orientations. Furthermore, PPL4 alone showed no effect on CaCO3 crystalization; however, PPL4 regulated the size of crystals collaborated with N-acetyl-D-glucosamine and chitin oligomer, which are specific in recognizing carbohydrates for PPL4. These observations highlight the unique functions and molecular evolution of this lectin family involved in the mollusk shell formation.
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3

Abhinav, Koyamangalath Vadakkepat, and Mamannamana Vijayan. "Structural diversity and ligand specificity of lectins. The Bangalore effort." Pure and Applied Chemistry 86, no. 9 (2014): 1335–55. http://dx.doi.org/10.1515/pac-2014-0607.

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AbstractStructural studies in this laboratory encompass four of the five major classes of plant lectins, including the one discovered by us. In addition to addressing issues specific to individual lectins, the work provided insights into protein folding, quaternary association and generation of ligand specificity. Legume and β-prism fold lectins constitute families of proteins in which small alterations in essentially the same tertiary structure lead to large variations in quaternary structure, including that involving an open structure. Strategies for generating ligand specificity include water bridges, variation in loop length, post translational modification and oligomerization. Three of the structural classes investigated have subunits with three-fold symmetry. The symmetry in the structure is reflected in the sequence to different extents in different sub-classes. The evolutionary implications of this observation have been explored. The work on lectins has now been extended to those from mycobacteria.
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4

Wood, Stephen D., Lisa M. Wright, Colin D. Reynolds, et al. "Structure of the native (unligated) mannose-specific bulb lectin from Scilla campanulata (bluebell) at 1.7 Å resolution." Acta Crystallographica Section D Biological Crystallography 55, no. 7 (1999): 1264–72. http://dx.doi.org/10.1107/s0907444999005326.

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The X-ray crystal structure of native Scilla campanulata agglutinin, a mannose-specific lectin from bluebell bulbs and a member of the Liliaceae family, has been determined by molecular replacement and refined to an R value of 0.186 at 1.7 Å resolution. The lectin crystallizes in space group P21212 with unit-cell parameters a = 70.42, b = 92.95, c = 46.64 Å. The unit cell contains eight protein molecules of Mr = 13143 Da (119 amino-acid residues). The asymmetric unit comprises two chemically identical molecules, A and B, related by a non-crystallographic twofold axis perpendicular to c. This dimer further associates by crystallographic twofold symmetry to form a tetramer. The fold of the polypeptide backbone closely resembles that found in the lectins from Galanthus nivalis (snowdrop) and Hippeastrum (amaryllis) and contains a threefold symmetric β-prism made up of three antiparallel four-stranded β-sheets. Each of the four-stranded β-sheets (I, II and III) possesses a potential saccharide-binding site containing conserved residues; however, site II has two mutations relative to sites I and III which may prevent ligation at this site. Our study provides the first accurate and detailed description of a native (unligated) structure from this superfamily of mannose-specific bulb lectins and will allow comparisons with a number of lectin–saccharide complexes which have already been determined or are currently under investigation.
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5

Sharma, Alok, Divya Chandran, Desh D. Singh та M. Vijayan. "Multiplicity of carbohydrate-binding sites in β-prism fold lectins: occurrence and possible evolutionary implications". Journal of Biosciences 32, S2 (2007): 1089–110. http://dx.doi.org/10.1007/s12038-007-0111-3.

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6

Sharma, Alok, та Mamannamana Vijayan. "Quaternary association in β-prism I fold plant lectins: Insights from X-ray crystallography, modelling and molecular dynamics". Journal of Biosciences 36, № 5 (2011): 793–808. http://dx.doi.org/10.1007/s12038-011-9166-2.

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7

Cornil, I., R. S. Kerbel, and J. W. Dennis. "Tumor cell surface beta 1-4-linked galactose binds to lectin(s) on microvascular endothelial cells and contributes to organ colonization." Journal of Cell Biology 111, no. 2 (1990): 773–81. http://dx.doi.org/10.1083/jcb.111.2.773.

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Cell surface carbohydrate structures acting as ligands for tissue specific mammalian lectins have been implicated in cell-cell interactions during embryogenesis, lymphocyte homing, and tumor cell metastasis. In this report, we provide evidence that beta 1-4 linked galactose (Gal) residues in N-linked oligosaccharides on the surface of blood born tumor cells serve as a ligand for binding to microvascular endothelial cells. D36W25, a class 1 glycosylation mutant of the MDAY-D2 lymphoreticular tumor cell line, lacks sialic acid and Gal in cellular glycans due to a defect in the Golgi UDP-Gal transporter. Using UDP-Gal and bovine galactosyltransferase in vitro, beta 1-4 Gal was restored to the surface of the cells and 70% of the galactosylated glycans persisted for 8 h in vitro at 37 degrees C. Compared to mock-treated D36W25 cells, galactosylated D36W25 cells showed an 80% increase in binding to microvascular endothelial cell monolayers in vitro. The enhanced binding of galactosylated D36W25 cells to endothelial cell was inhibited by the addition of lactosamine-conjugated albumin to the assay. Consistent with these observations, swainsonine and castinospermine, two inhibitors of N-linked processing that result in loss of lactosamine antennae inhibited the binding of wild-type MDAY-D2 cells to endothelial cells in vitro. Injection of radiolabeled tumor cells into the circulation of syngeneic mice, showed that galactosylation of D36W25 cells resulted in 2-3 more tumor cells retained in the lungs and livers. In addition, galactosylation of D36W25 cells increased by 30-fold the number of visible liver metastases on inspection 4 wk after tumor cell injection. These results suggest that beta 1-4Gal-binding lectins on microvascular endothelial cells can contribute to retention and secondary tumor formation of blood born tumor cells. With the increasing availability of purified glycosyltransferases, reconstruction of a variety of carbohydrate sequences on the surface of class 1 mutants provides a controlled means of studying carbohydrate-lectin interactions on viable cells.
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8

Naganuma, Takako, Wataru Hoshino, Yukihiro Shikanai та ін. "Novel Matrix Proteins of Pteria penguin Pearl Oyster Shell Nacre Homologous to the Jacalin-Related β-Prism Fold Lectins". PLoS ONE 9, № 11 (2014): e112326. http://dx.doi.org/10.1371/journal.pone.0112326.

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9

Kumazawa-Inoue, Kaori, Tomoko Mimura, Sachiko Hosokawa-Tamiya та ін. "ZG16p, an animal homolog of β-prism fold plant lectins, interacts with heparan sulfate proteoglycans in pancreatic zymogen granules". Glycobiology 22, № 2 (2011): 258–66. http://dx.doi.org/10.1093/glycob/cwr145.

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10

Clerch, L. B., P. L. Whitney, and D. Massaro. "Rat lung lectin synthesis, degradation and activation. Developmental regulation and modulation by dexamethasone." Biochemical Journal 245, no. 3 (1987): 683–90. http://dx.doi.org/10.1042/bj2450683.

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Soluble lectins are widely distributed cell-agglutinating proteins. Their activity is developmentally regulated in several tissues, including the lung, but virtually nothing is known about the mechanisms of the developmental regulation or the turnover of these proteins. We studied mechanisms that might be responsible for the developmentally regulated changes in the activity of a lectin (beta-galactoside-binding protein) found in the lung, and determined if its activity or turnover could be modulated by treatment of rat pups with a glucocorticosteroid hormone (dexamethasone). Our studies on the activity and turnover of the lectin indicated that the peak of lectin activity (units/mg of protein) that occurred at age 12 days appeared to be brought about by two means: an increase in the activity of the lectin molecule itself (units/micrograms of lectin) that occurred at age 8 days, and 1.5-fold increase in the absolute rate of lectin synthesis at age 11 days. The decline in lectin activity was associated with a decrease in its rate of synthesis, return to the baseline extent of activation, and an increased rate of degradation. Treatment of rat pups with dexamethasone diminished the peak of lectin activity (units/mg of protein) by about 25%. This effect of dexamethasone was due, at least in part, to the complete prevention of activation of the lectin molecule (units/micrograms of lectin) and a premature increase in the rate of lectin degradation. Perhaps the normal fall in lectin activity after age 11 days is caused by mechanisms induced by the increase in serum corticosteroid that occurs at that age.
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