By Gerardo R. Vasta PhD, Hafiz Ahmed PhD
Introduces Groundbreaking ways for Assessing Lectin Function
Lectins and their ligands are below rather a heavy microscope because of their capability functions to pharmacology, immunology, melanoma remedy, and agriculture. With turning out to be curiosity within the glycobiology box, the physique of study regarding lectin roles has grown at an explosive cost, rather long ago twenty years. Animal Lectins: A useful View provides the main up to date research of those carbohydrate-binding, and probably lifesaving, proteins in a single accomplished 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
- Cell-cell interactions and signaling
Describes the Structural foundation of Protein-Carbohydrate Interactions
Under the editorial assistance of 2 top protein chemistry specialists and with contributions from well-recognized box professionals, this ebook logically and systematically discusses either intracellular and extracellular lectin features. it really is an important springboard for destiny box examine and a transparent and concise wisdom base that glycobiology, biochemistry, and immunology researchers can't come up with the money for to be without.
Read or Download Animal Lectins: A Functional View PDF
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Extra resources for Animal Lectins: A Functional View
1974 The isolation and properties of a rabbit liver binding protein specific for asialoglycoproteins. J. Biol. Chem. 249, 5536–5543. 15. , and Resheff, G. 1975 A β-Dgalactoside binding protein from electric organ tissue of Electrophorus electricus. Proc. Natl Acad. Sci. USA 72, 1383–1387. 16. I. J. 1965 Specific binding of concanvalin A to cross-linked dextran gels. Biochem. J. 96, 23C–25C. 17. M. 2001 The ABO blood group system: Historical background. Transfus. Med. 11, 243–265. 18. Kocourek, J.
3A). The cation is coordinated with seven oxygen atoms from the main chain or side chain of six residues: Asn35 (O), Asp38 (Oδ1), Asn40 (O), Ser49 (O, Oγ1), Cys146 (O), and Glu147. , 1997). 4 (See color insert following blank page 170. ) Structure of F-lectins. (A) Overall structure. The two β-sheets that form the core of the molecule are clearly visible. The carbohydrate complementarity determining regions (CDRs) are indicated. (B) Fucose recognition. Residues that interact with the fucose ligand are shown and the H-bonds to the sugar indicated.
L. 1998 The ice-binding site of Atlantic herring antifreeze protein corresponds to the carbohydrate-binding site of C-type lectins. Biochemistry 37, 4080–4085. 23. Drickamer, K. B. 1999 C-Type lectin-like domains in Caenorhabditis elegans: Predictions from the complete genome sequence. Glycobiology 9, 1357–1369. 24. N. 2002 Galectinomics: Finding themes in complexity. Biochim. Biophys. Acta. 1572, 209–231. 25. M. 2002 Identification of a fold common to a family of innate immunity recognition factors: Structure of a fucolectin from the European eel (Anguilla anguilla).