title: Lectins: getting familiar with translators of the sugar code.
abstract: The view on the significance of the presence of glycans in glycoconjugates is undergoing a paradigmatic change. Initially mostly considered to be rather inert and passive, the concept of the sugar code identifies glycans as highly versatile platform to store information. Their chemical properties endow carbohydrates to form oligomers with unsurpassed structural variability. Owing to their capacity to engage in hydrogen (and coordination) bonding and C-H/π-interactions these "code words" can be "read" (in Latin, legere) by specific receptors. A distinct class of carbohydrate-binding proteins are the lectins. More than a dozen protein folds have developed carbohydrate-binding capacity in vertebrates. Taking galectins as an example, distinct expression patterns are traced. The availability of labeled endogenous lectins facilitates monitoring of tissue reactivity, extending the scope of lectin histochemistry beyond that which traditionally involved plant lectins. Presentation of glycan and its cognate lectin can be orchestrated, making a glycan-based effector pathway in growth control of tumor and activated T cells possible. In order to unravel the structural basis of lectin specificity for particular glycoconjugates mimetics of branched glycans and programmable models of cell surfaces are being developed by strategic combination of lectin research with synthetic and supramolecular chemistry.
authors.affiliation: Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University, Veterinärstr. 13, 80539 Munich, Germany. Sabine.Andre@lmu.de.
authors.forename: Sabine
authors.initials: S
authors.lastname: André
authors.affiliation: Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University, Veterinärstr. 13, 80539 Munich, Germany. kaltner@lmu.de.
authors.forename: Herbert
authors.initials: H
authors.lastname: Kaltner
authors.affiliation: Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University, Veterinärstr. 13, 80539 Munich, Germany. j.manning@lmu.de.
authors.forename: Joachim C
authors.initials: JC
authors.lastname: Manning
authors.affiliation: School of Chemistry, National University of Ireland Galway, University Road, Galway, Ireland. paul.v.murphy@nuigalway.ie.
authors.forename: Paul V
authors.initials: PV
authors.lastname: Murphy
authors.affiliation: Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University, Veterinärstr. 13, 80539 Munich, Germany. gabius@lectins.de.
authors.forename: Hans-Joachim
authors.initials: HJ
authors.lastname: Gabius
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002240:Carbohydrate Sequence; D006023:Glycoproteins / Q000737:chemistry / Q000502:physiology; D006801:Humans; D037102:Lectins / Q000737:chemistry / Q000502:physiology*; D008969:Molecular Sequence Data; D011134:Polysaccharides / Q000737:chemistry / Q000502:physiology*; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: D006023:Glycoproteins; D037102:Lectins; D011134:Polysaccharides