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 because of their strength purposes to pharmacology, immunology, melanoma treatment, and agriculture. With turning out to be curiosity within the glycobiology box, the physique of study on the topic of lectin roles has grown at an explosive price, fairly some time past twenty years. Animal Lectins: A useful View offers the main updated research of those carbohydrate-binding, and probably lifesaving, proteins in a single finished 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 prime protein chemistry specialists and with contributions from well-recognized box specialists, this publication logically and systematically discusses either intracellular and extracellular lectin features. it truly is an important springboard for destiny box learn and a transparent and concise wisdom base that glycobiology, biochemistry, and immunology researchers can't come up with the money for to be without.

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Additional info for Animal Lectins: A Functional View

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2) of galectin-7 shows that dimerization of this lectin is very different from those of dimeric galectins. , 1998; Rini and Lobsanov, 1999). 3 CARBOHYDRATE-BINDING SPECIFICITY OF GALECTINS THEIR CARBOHYDRATE-BINDING SITES AND The ability of galectins to discriminate among carbohydrate structures is striking. , 1990, 1996, 2004). For most galectins, LacNAc and thiodigalactoside (TDG) are 5–10 times more active than Lac. In general, the 4¢-OH, 6¢-OH groups of the Gal residue of Lac/LacNAc are critical for binding, and thus, any changes (epimers or substitutions) of these hydroxyls reduces binding efficiency.

Pneumoniae OMe-GalNAc GlcNac Man-6-P Man-6-P Earthworm Crab B. taurus B. taurus A. anguilla Striped Bass 9/6/2008 2:23:29 PM Structural Aspects of Lectin–Ligand Interactions 17 The C-terminal region of the double loop binds carbohydrate in a shallow depression made by three stretches of residues S1, S2, and S3 in a S1–S3–S2 sequence, surrounded by five loops. 4B). S1 contains the motif [E/Q] P[N/D]X6E, S2 contains the conserved Cys, and S3 a WNDX2C motif. This highly conserved and more hydrophilic portion of the fold is stabilized by one conserved disulfide bridge that joins the onset of S2 and the end of S3.

All Siglecs are extracellular receptors consisting of one Ig-V domain, followed by a variable number (1–16) of Ig-C domains, a transmembrane region consisting of a single transmembrane helix, a short cytoplasmic domain, in some cases two or more immunoreceptor tyrosine-based inhibitory motifs (ITIMs), [I/V]XYXXL). The Ig-V domain contains the carbohydrate-binding site and the ensuing Ig-C domains appear to function as spacers separating the carbohydrate binding site from the membrane. The first domain contains several residues that are well-conserved in Siglecs: an arginine residue that forms a salt bridge with the carboxyl group of sialic acid, two aromatic residues (one near the N-terminal and the other after the conserved arginine), and three cysteines, one of which forms an unusual interdomain disulfide bridge with a cysteine in the second Ig domain.

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