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5. Engineered carbohydrate-recognition domains for glycoproteomic analysis of cell surface glycosylation and ligands for glycan-binding receptors.

Author

Powlesland AS, Quintero-Martinez A, Lim PG, Pipirou Z, Taylor ME, and Drickamer K

Subjects
Amino Acid Sequence, Animals, Glycosylation, Humans, Lectins chemistry, Ligands, Membrane Glycoproteins analysis, Membrane Glycoproteins chemistry, Membrane Glycoproteins metabolism, Models, Molecular, Molecular Sequence Data, Protein Binding, Carbohydrate Metabolism physiology, Lectins metabolism, Membrane Glycoproteins chemical synthesis, Protein Engineering methods, Protein Interaction Domains and Motifs, Proteomics methods
Abstract

Modular calcium-dependent carbohydrate-recognition domains (CRDs) of mammalian glycan-binding receptors (C-type lectins), engineered to have novel glycan-binding selectivity, have been developed as tools for the study of glycans on cell surfaces. Structure-based specificity swapping between domains can be complemented by empirical characterization of ligand-binding specificity using glycan arrays. Both natural and modified CRDs can be used as probes for detecting and isolating glycoproteins that bear specific glycan epitopes and that act as target ligands for glycan-binding receptors. CRD-based affinity chromatography facilitates proteomic and glycomic analysis of such ligands., (Copyright (c) 2010 Elsevier Inc. All rights reserved.)

Published
2010
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