Crystal Structure of Mistletoe Lectin I fromViscum album

Krauspenhaar, R.; Eschenburg, Susanne; Perbandt, Markus; Kornilov, V. V.; Konareva, N. V.; Mikailova, I.; Stoeva, Stanka; Wacker, Roland; Maier, Timm; Singh, T.P.; Mikhailov, A.M.; Voelter, Wolfgang; Betzel, Christian

doi:10.1006/bbrc.1999.0470

Cited by 61 publications

(38 citation statements)

References 28 publications

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“…related to ribosome inactivation. 9,23,24,25 Currently, there is no evidence that the natural biological function of MOA is coupled to toxic activity; what is intriguing, however, is the apparent resemblance between the C-terminal domain of MOA and various catalytically active proteins, such as certain glycanases and proteases. This structural similarity is especially apparent in the active site cleft, and extends to the great similarity of the catalytic triad as well as to several additional important residues in the cleft of these enzymes.…”

Section: Discussionmentioning

confidence: 99%

Crystal Structure of the Marasmius Oreades Mushroom Lectin in Complex with a Xenotransplantation Epitope

Grahn

Askarieh

Holmner

et al. 2007

Journal of Molecular Biology

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Section: Discussionmentioning

confidence: 99%

Crystal Structure of the Marasmius Oreades Mushroom Lectin in Complex with a Xenotransplantation Epitope

Grahn

Askarieh

Holmner

et al. 2007

Journal of Molecular Biology

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“…Crystallized by Krauspenhaar et al (1999), miseltoe lectin ML-I from Viscum album showed that the overall protein fold is similar to that of ricin from Ricinus communis. Figure 3 shows the stereo view of mistletoe (Viscum album) lectin I (MLI) interface region between two B-chain domain 1s, a type II ribosome inactivating protein that exists as a [AB]-2 dimer.…”

Section: Structurementioning

confidence: 94%

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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“…The biological importance of MLI as a dimeric cytotoxic type‐II RIP is also discussed and details of the dimer interface are analysed. The availability of the known structure of MLI without a specific sugar [25] (pdb 1ce7, 2mll) has enabled us to make a comparison with the present structure.…”

mentioning

confidence: 99%

Crystal structure at 3 Å of mistletoe lectin I, a dimeric type‐II ribosome‐inactivating protein, complexed with galactose

Niwa

Tonevitsky

Агапов

et al. 2003

European Journal of Biochemistry

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The X-ray structure of mistletoe lectin I (MLI), a type-II ribosome-inactivating protein (RIP), cocrystallized with galactose is described. The model was refined at 3.0 Å resolution to an R-factor of 19.9% using 21 899 reflections, with R free 24.0%. MLI forms a homodimer (A-B) 2 in the crystal, as it does in solution at high concentration. The dimer is formed through contacts between the N-terminal domains of two B-chains involving weak polar and nonpolar interactions. Consequently, the overall arrangement of sugar-binding sites in MLI differs from those in monomeric type-II RIPs: two N-terminal sugar-binding sites are 15 Å apart on one side of the dimer, and two C-terminal sugarbinding sites are 87 Å apart on the other side. Galactose binding is achieved by common hydrogen bonds for the two binding sites via hydroxy groups 3-OH and 4-OH and hydrophobic contact by an aromatic ring. In addition, at the N-terminal site 2-OH forms hydrogen bonds with Asp27 and Lys41, and at the C-terminal site 3-OH and 6-OH undergo water-mediated interactions and C5 has a hydrophobic contact. MLI is a galactose-specific lectin and shows little affinity for N-acetylgalactosamine. The reason for this is discussed. Structural differences among the RIPs investigated in this study (their quaternary structures, location of sugar-binding sites, and fine sugar specificities of their B-chains, which could have diverged through evolution from a two-domain protein) may affect the binding sites, and consequently the cellular transport processes and biological responses of these toxins.

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Crystal Structure of Mistletoe Lectin I fromViscum album

Cited by 61 publications

References 28 publications

Crystal Structure of the Marasmius Oreades Mushroom Lectin in Complex with a Xenotransplantation Epitope

Crystal Structure of the Marasmius Oreades Mushroom Lectin in Complex with a Xenotransplantation Epitope

Lectins as Bioactive Plant Proteins: A Potential in Cancer Treatment

Crystal structure at 3 Å of mistletoe lectin I, a dimeric type‐II ribosome‐inactivating protein, complexed with galactose

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