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

By Gerardo R. Vasta PhD, Hafiz Ahmed PhD

Introduces Groundbreaking ways for Assessing Lectin Function

Lectins and their ligands are less than particularly a heavy microscope as a result of their capability functions to pharmacology, immunology, melanoma treatment, and agriculture. With growing to be curiosity within the glycobiology box, the physique of analysis concerning lectin roles has grown at an explosive expense, quite some time past two decades. Animal Lectins: A useful View offers the main up to date research of those carbohydrate-binding, and almost certainly lifesaving, proteins in a single entire quantity.

This standard-setting source provides 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 tips of 2 top protein chemistry specialists and with contributions from well-recognized box experts, this booklet logically and systematically discusses either intracellular and extracellular lectin capabilities. it really is an important springboard for destiny box learn and a transparent and concise wisdom base that glycobiology, biochemistry, and immunology researchers can't manage to pay for to be without.

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Extra resources for Animal Lectins: A Functional View

Sample text

Serum ficolins play an important role as pattern recognition molecules in innate immunity by complexing with serine proteases termed MASPs. Upon binding to carbohydrates on the surfaces of microbial pathogens, serum ficolins eliminate them by direct opsonization. In Chapter 35, Hatakeyama describes characteristic features of a Ca2+-dependent, Gal/GalNAcspecific lectin (CEL-III) from the sea cucumber (Cucumaria echinata) and its putative mechanism of hemolytic activity on the basis of the structural information.

Other proteins that lack carbohydrate-binding properties also contain C-type lectin-like domains (CTLDs), suggesting that this domain is a characteristic of a larger protein superfamily (Drickamer, 1993). Nevertheless, we are going to focus this presentation on a subset of these proteins with carbohydrate-binding properties. 2); in those, the regular elements of secondary structure are conserved with changes concentrated in the loops connecting these elements. 1 (See color insert following blank page 170.

D) Computer model of H type 1 trisaccharide bound to the AAA binding site. The model predicts interactions between the third carbohydrate moiety and the CDR1. horseshoe-crab F-lectin, shows a fourfold enhancement of its hemagglutination activity for A-type erythrocytes upon the addition of Ca2+. , 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.

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