作者: Hans-Joachim Gabius , Sabine André , Jesús Jiménez-Barbero , Antonio Romero , Dolores Solís
DOI: 10.1016/J.TIBS.2011.01.005
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摘要: Lectins are carbohydrate-binding proteins which lack enzymatic activity on their ligand and distinct from antibodies free mono- oligosaccharide sensor/transport proteins. Emerging insights into the functional dimension of lectin binding to cellular glycans have strongly contributed shaping 'sugar code'. Fittingly, over a dozen folds broad spectrum site architecture, ranging shallow grooves deep pockets, developed sugar-binding capacity. A central question is how exquisite target specificity endogenous lectins for certain can be explained. In this regard, affinity regulation first systematically dissected six levels. Experimentally, strategic combination methods monitor aspects lectin-glycan interplay offers promising perspective answer question.