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Lectin-carbohydrate analysis by molecular dynamics: Parkia lectins case study.
An Acad Bras Cienc
December 2024
Universidade Federal do Ceará, Departamento de Bioquímica e Biologia Molecular, Laboratório de Moléculas Biologicamente Ativas, Rua José Aurelio Camara, s/n, 60440-970 Fortaleza, CE, Brazil.
Understanding lectin-carbohydrate interactions at the structural and molecular levels is crucial to the field of lectins, as the diverse roles and biological activities exhibited by these proteins are fundamentally linked to their specific binding to target glycoconjugates. This study aimed to apply molecular dynamics to analyze the structure and binding properties of Parkia lectins. 3D structures of Parkia platycephala and P.
View Article and Find Full Text PDFMultivalent lectin-carbohydrate interactions: Energetics and mechanisms of binding.
Adv Carbohydr Chem Biochem
November 2023
Department of Molecular Pharmacology, Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY, United States.
The biological signaling properties of lectins, which are carbohydrate-binding proteins, are due to their ability to bind and cross-link multivalent glycoprotein receptors on the surface of normal and transformed cells. While the cross-linking properties of lectins with multivalent carbohydrates and glycoproteins are relatively well understood, the mechanisms of binding of lectins to multivalent glycoconjugates are less well understood. Recently, the thermodynamics of binding of lectins to synthetic clustered glycosides, a multivalent globular glycoprotein, and to linear glycoproteins (mucins) have been described.
View Article and Find Full Text PDFA reference genome for the long-term kleptoplast-retaining sea slug Elysia crispata morphotype clarki.
G3 (Bethesda)
December 2023
Department of Biochemistry, Purdue University, West Lafayette, IN 47907, USA.
Several species of sacoglossan sea slugs possess the incredible ability to sequester chloroplasts from the algae they consume. These "photosynthetic animals" incorporate stolen chloroplasts, called kleptoplasts, into the epithelial cells of tubules that extend from their digestive tracts throughout their bodies. The mechanism by which these slugs maintain functioning kleptoplasts in the absence of an algal nuclear genome is unknown.
View Article and Find Full Text PDFStructure and interactions of the phloem lectin (phloem protein 2) Cus17 from Cucumis sativus.
Structure
April 2023
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India. Electronic address:
Phloem protein 2 (PP2) contributes crucially to phloem-based defense in plants by binding to carbohydrates displayed by pathogens. However, its three-dimensional structure and the sugar binding site remained unexplored. Here, we report the crystal structure of the dimeric PP2 Cus17 from Cucumis sativus in its apo form and complexed with nitrobenzene, N-acetyllactosamine, and chitotriose.
View Article and Find Full Text PDFWild Mushroom Extract as Lectin Source for Engineering a Lactose Photoelectrochemical Biosensor.
Biosensors (Basel)
February 2023
Centro de Ciência e Tecnologia, Universidade Federal do Cariri, Juazeiro do Norte 63048-080, CE, Brazil.
mushroom biomass contains a lectin, ABL, with remarkable specificity for lactose biorecognition; in this work, this feature was explored to develop a photoelectrochemical biosensor. The high lectin activity found in saline extracts of this macrofungus (640 HU mL), even at critical pH values (4-10) and temperatures (20-100 °C), allowed its direct use as an ABL source. Theoretical and experimental evidence revealed favorable electrostatic and biocompatible conditions to immobilize ABL on a poly(methylene blue)/fluorine-doped tin oxide-coated glass platform, giving rise to the ABL/PMB/FTO biosensor.
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