Abstract
The genetic code connects the two biochemical dimensions of nucleic acids and proteins. Theoretical calculations on coding capacity reveal that oligo saccharides as hardware surpass peptides by more than seven orders of magnitude based on hexamer synthesis. Thus, the sugar code establishes the third dimension of biological information transfer. Using carbohy-drate-binding proteins (lectins, enzymes and antibodies) the information content of such epi-topes is decoded. Currently, five families of animallectins are defined in structural terms, i.e. the C-type, I-type and P-type groups, the galectins and the pentraxins. They are involved in intra-and intercellular glycan routing using oligo saccharides as postal-code equivalents and acting as defense molecules homing in on foreign or aberrant glycosignatures, as crosslinking agent in biosignaling and as coordinator of transient or firm cell-ceIVcell-matrix contacts. By delineating the driving forces toward complex formation, knowledge about the causes for specificity can be turned into design of custom-made high-affinity ligands for clinical applica-tion, e.g. in anti-adhesion therapy, drug targeting or diagnostic histopathology.
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Kaltner, H., Gabius, HJ. (2001). Animal Lectins: from Initial Description to Elaborated Structural and Functional Classification. In: Wu, A.M. (eds) The Molecular Immunology of Complex Carbohydrates —2. Advances in Experimental Medicine and Biology, vol 491. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1267-7_6
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DOI: https://doi.org/10.1007/978-1-4615-1267-7_6
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