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Title

From lectin structure to functional glycomics: principles of the sugar code

AuthorsGabius, Hans-Joachim; André, Sabine; Jiménez-Barbero, Jesús ; Romero, Antonio ; Solís, Dolores
KeywordsBOVINE HEART GALECTIN-1
MISTLETOE LECTIN
MISTLETOE LECTIN
LIGAND-BINDING
CELL-SURFACE
MOLECULAR-DYNAMICS
NMR-SPECTROSCOPY
ANIMAL LECTINS
CROSS-LINKING
FORCE-FIELD
SOLID-PHASE
Issue DateJun-2011
PublisherElsevier
CitationTrends Biochem.Sci.36(6):298-313(2011)
AbstractLectins 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.
Description16 pág.; 7 figuras; Material suplementario: 3 tablas;dx.doi.org/10.1016/j.tibs.2011.01.005
Publisher version (URL)https://doi.org/10.1016/j.tibs.2011.01.005
URIhttp://hdl.handle.net/10261/47631
ISSN0968-0004
E-ISSN0167-7640
Appears in Collections:(CIB) Artículos
(IQFR) Artículos
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