Gerardo R. Vasta PhD, Hafiz Ahmed PhD's Animal Lectins: A Functional View PDF

By Gerardo R. Vasta PhD, Hafiz Ahmed PhD

ISBN-10: 0849372690

ISBN-13: 9780849372698

ISBN-10: 1420006975

ISBN-13: 9781420006971

Introduces Groundbreaking methods for Assessing Lectin Function

Lectins and their ligands are less than fairly a heavy microscope because of their capability functions to pharmacology, immunology, melanoma treatment, and agriculture. With starting to be curiosity within the glycobiology box, the physique of analysis on the topic of lectin roles has grown at an explosive cost, rather long ago twenty years. Animal Lectins: A practical View offers the main up to date research of those carbohydrate-binding, and possibly lifesaving, proteins in a single finished quantity.

This standard-setting source offers new insights into the organic roles of so much animal lectins, together with their functionality in an infection prevention via innate immunity. It additionally discusses such lectin behaviors as:

  • Glycoprotein folding
  • Sorting and targeting
  • Cell adhesion
  • Embryogenesis
  • Cell-cell interactions and signaling

Describes the Structural foundation of Protein-Carbohydrate Interactions

Under the editorial suggestions of 2 prime protein chemistry specialists and with contributions from well-recognized box gurus, this ebook logically and systematically discusses either intracellular and extracellular lectin features. it really is a necessary springboard for destiny box study and a transparent and concise wisdom base that glycobiology, biochemistry, and immunology researchers can't have the funds for to be without.

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Additional info for Animal Lectins: A Functional View

Sample text

H. 1988 Bifunctional properties of lectins: Lectins redefined. Trends Biochem. Sci. 13, 480–482. 2. L. 1899 Recherches experimentales sur une agglutinine produite par la glande de l’albumen chez l’Helix pomatia. R. Acad. Sci. 129, 233. 3. M. and Robin, C. 1853 Observation de leocythemie. C. R. Mem. Soc. Biol. 5, 44–50. 4. Leyden, E. 1872 Zur Kenntniss des bronchial-asthma. Arch. Pathol. Anat. 54, 324–344. 5. R. 8 A° resolution. Biochemistry 38, 13837–13843. 6. Flexner, S. and Noguchi, H. 1902 Snake venom in relation to haemolysis, bacteriolysis, and toxicity.

1997), may result from possible changes induced by cation binding of the conformation of the contiguous loops CDR1 and CDR2, which are involved in binding of the ligand. 4B). A network of hydrogen bonds maintains this triad of residues in optimal positions at the center of the hollow to recognize the axial 4-OH group of the fucose with hydrogen bonds in a perfect tetrahedral geometry. In addition, the arginine residues of the triad recognize O5 and the equatorial 3-OH group of the Fuc. Two hydrophobic patches provide van der Waals contacts to the monosaccharide: its ring atoms C1 and C2 rest over a rare disulfide bridge between consecutive cysteine residues and its C6 docks loosely in a hydrophobic pocket, stacking against the rings of His27 and Phe45.

The long sequence motif characteristic of C-lectins shows the conserved residues in blue, the cysteines in green, and the conserved proline in red. The two disulfide bridges that connect the cysteines are shown by the thick magenta lines. (B) Overall structure. The structure of the C-lectin CRD is the small α/β module shown in the figure using the PDB 1RLD. The three Ca2+ are shown as green spheres. At the top of the CRD, the binding site for ligand is shown occupied by mannose. (C) Mannose bound to a C-lectin.

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Animal Lectins: A Functional View by Gerardo R. Vasta PhD, Hafiz Ahmed PhD


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