Structure of a legume lectin from the bark of <i>Robinia pseudoacacia</i> and its complex with N‐acetylgalactosamine

Rabijns, A.; Verboven, Christel; Rougé, Pierre; Barre, Annick; Damme, Els J.M. Van; Peumans, Willy J.; Ranter, C. J. De

doi:10.1002/prot.1112

Cited by 27 publications

(18 citation statements)

References 31 publications

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“…The CϭO group is hydrogen bonded to the NH backbone of Ala 106 . This orientation of GalNAc, together with specific hydrogen bond and hydrophobic interactions of the N-acetyl group, is similar to that observed in the crystal structures of Dolichos biflorus seed lectin (13) and Robinia pseudoacacia bark lectin (32).…”

Section: Structural Basis For the Specificity Differences Between Gs supporting

confidence: 83%

Isolectins I-A and I-B of Griffonia(Bandeiraea) simplicifolia

Lescar

Loris

Mitchell

et al. 2002

Journal of Biological Chemistry

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Seeds from the African legume shrub Griffonia simplicifolia contain several lectins. Among them the tetrameric lectin GS I-B 4 has strict specificity for terminal ␣Gal residues, whereas the closely related lectin GS I-A 4 can also bind to ␣GalNAc. These two lectins are commonly used as markers in histology or for research in xenotransplantation. To elucidate the basis for the fine difference in specificity, the amino acid sequences of both lectins have been determined and show 89% identity. The crystal structure of GS I-B 4 , determined at 2.5-Å resolution, reveals a new quaternary structure that has never been observed in other legume lectins. An unexpected loss of both Ca

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Section: Structural Basis For the Specificity Differences Between Gs supporting

confidence: 83%

Isolectins I-A and I-B of Griffonia(Bandeiraea) simplicifolia

Lescar

Loris

Mitchell

et al. 2002

Journal of Biological Chemistry

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“…The stability of a lectin depends on its tertiary (legume lectin fold) or quaternary structure and on some additional and unique features (Rabijns et al, 2001). The characterization of the primary structure, isoforms, and molecular modeling of lectins is currently a very active research field (Stoeva et al, 2001).…”

Section: Structurementioning

confidence: 99%

Lectins as Bioactive Plant Proteins: A Potential in Cancer Treatment

Mejı́a

Prisecaru

2005

Critical Reviews in Food Science and Nutrition

292

159

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Plant lectins, a unique group of proteins and glycoproteins with potent biological activity, occur in foods like wheat, corn, tomato, peanut, kidney bean, banana, pea, lentil, soybean, mushroom, rice, and potato. Thus, dietary intakes by humans can be significant. Many lectins resist digestion, survive gut passage, and bind to gastrointestinal cells and/or enter the circulation intact, maintaining full biological activity. Several lectins have been found to possess anticancer properties in vitro, in vivo, and in human case studies; they are used as therapeutic agents, preferentially binding to cancer cell membranes or their receptors, causing cytotoxicity, apoptosis, and inhibition of tumor growth. These compounds can become internalized into cells, causing cancer cell agglutination and/or aggregation. Ingestion of lectins also sequesters the available body pool of polyamines, thereby thwarting cancer cell growth. They also affect the immune system by altering the production of various interleukins, or by activating certain protein kinases. Lectins can bind to ribosomes and inhibit protein synthesis. They also modify the cell cycle by inducing non-apoptotic G1-phase accumulation mechanisms, G2/M phase cell cycle arrest and apoptosis, and can activate the caspase cascade. Lectins can also downregulate telomerase activity and inhibit angiogenesis. Although lectins seem to have great potential as anticancer agents, further research is still needed and should include a genomic and proteomic approach.

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“…33 The stability and resistance to degradation of soybean lectins depend on its tertiary and quaternary structures. [34][35][36] The structure of SBA monomer is shown in Figure 2.…”

Section: Lectins: Structure Binding Speci Cities and Physiologic Efmentioning

confidence: 99%

The Anticarcinogenic Potential of Soybean Lectin and Lunasin

2003

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Cancer is one of the leading causes of death worldwide, generally exceeded only by cardiovascular disease in the developed world. The number of people diagnosed with cancer within the next few decades is expected to double. There will therefore be increased demand for novel diagnostic and medical therapies that use new non-traditional sources. Soybeans contain a variety of anticarcinogenic phytochemicals. Recently, there has been increased interest in the potential health benefits of bioactive polypeptides and proteins from soybeans, including lunasin and lectins. Lunasin is a polypeptide that arrests cell division and induces apoptosis in malignant cells. Lectins are glycoproteins that selectively bind carbohydrates; lectins are used in medicine in a variety of new applications. Additional research, including clinical trials, should continue to examine and elucidate the therapeutic effects, nutritional benefits, and toxic consequences of commonly ingested soybean lectins and lunasin.

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Structure of a legume lectin from the bark of Robinia pseudoacacia and its complex with N‐acetylgalactosamine

Cited by 27 publications

References 31 publications

Isolectins I-A and I-B of Griffonia(Bandeiraea) simplicifolia

Isolectins I-A and I-B of Griffonia(Bandeiraea) simplicifolia

Lectins as Bioactive Plant Proteins: A Potential in Cancer Treatment

The Anticarcinogenic Potential of Soybean Lectin and Lunasin

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