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

By Gerardo R. Vasta PhD, Hafiz Ahmed PhD

ISBN-10: 0849372690

ISBN-13: 9780849372698

ISBN-10: 1420006975

ISBN-13: 9781420006971

Introduces Groundbreaking ways for Assessing Lectin Function

Lectins and their ligands are lower than really a heavy microscope as a result of their strength functions to pharmacology, immunology, melanoma treatment, and agriculture. With transforming into curiosity within the glycobiology box, the physique of study on the topic of lectin roles has grown at an explosive cost, really long ago twenty years. Animal Lectins: A practical View provides the main up to date research of those carbohydrate-binding, and possibly lifesaving, proteins in a single entire quantity.

This standard-setting source provides new insights into the organic roles of such a lot 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 information of 2 major protein chemistry specialists and with contributions from well-recognized box specialists, this publication logically and systematically discusses either intracellular and extracellular lectin capabilities. it really is a vital 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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Extra resources for Animal Lectins: A Functional View

Example text

Although the crystal structure of AAA shows a protomer per asymmetric unit, the crystal belongs to a space group (R32) that includes a threefold symmetry. This fact and the area buried by the trimer generated by application of the threefold suggest that the trimer present in the crystal is physiological. Since the function of lectins is to bind surface glycans in a multivalent fashion, the proposed trimer of the AAA–fucose complex provides the basis for understanding the function of this protein in innate immunity.

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. J. Exp. Med. 6, 277–301. 7. C. and Green, C. 1992 Lectins as blood typing reagents. In: Franz, H. ), Advances in Lectin Research, Vol. 5. Ullstein Mosby, Berlin, pp. 51–94. 8. Noguchi, H. 1903 On the multiplicity of the serum haemagglutinins of cold-blooded animals. Zentralbl. Bakteriol. Abt. l Orig. 34, 286. 9. Cantacuzene, J.

Similar arrangement of protomers has been observed in the crystal structure F-lectin from Stripped Bass (MsFPB2; Bianchet, Odom, Amzel, and Vasta, private communication). , 1995). 4B) correlates with the activity against negatively charged liposaccharides present in bacterial membranes. 5 IG-TYPE LECTINS (SIGLECS) One unusual, and may be surprising, family of carbohydrate binding proteins are the Ig-type lectins (Amzel and Poljak, 1979). The carbohydrate-binding module of Ig-type lectins is a single immunoglobulin fold (Ig) domain.

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