title: From lectin structure to functional glycomics: principles of the sugar code.
abstract: Lectins are carbohydrate-binding proteins which lack enzymatic activity on their ligand and are distinct from antibodies and free mono- and oligosaccharide sensor/transport proteins. Emerging insights into the functional dimension of lectin binding to cellular glycans have strongly contributed to the shaping of the 'sugar code'. Fittingly, over a dozen folds and a broad spectrum of binding site architecture, ranging from shallow grooves to deep pockets, have developed sugar-binding capacity. A central question is how the exquisite target specificity of endogenous lectins for certain cellular glycans can be explained. In this regard, affinity regulation is first systematically dissected into six levels. Experimentally, the strategic combination of methods to monitor distinct aspects of the lectin-glycan interplay offers a promising perspective to answer this question.
authors: Institute of Physiological Chemistry, Ludwig-Maximilians-University Munich, München, Germany. gabius@tiph.vetmed.uni-muenchen.de
authors: Hans-Joachim
authors: HJ
authors: Gabius
authors: Sabine
authors: S
authors: André
authors: Jesús
authors: J
authors: Jiménez-Barbero
authors: Antonio
authors: A
authors: Romero
authors: Dolores
authors: D
authors: Solís
mesh_terms: D002241:Carbohydrates / Q000737:chemistry*; D054794:Glycomics; D037102:Lectins / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation
chemical_list: D002241:Carbohydrates; D037102:Lectins