Engineered carbohydrate-recognition domains for glycoproteomic analysis of cell surface glycosylation and ligands for glycan-binding receptors.
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.
Powlesland
Alex S
AS
Division of Molecular Biosciences, Department of Life Sciences, Imperial College, Biochemistry Building, London, United Kingdom.
Quintero-Martinez
Adrián
A
Lim
Paik Gee
PG
Pipirou
Zoi
Z
Taylor
Maureen E
ME
Drickamer
Kurt
K
D000595:Amino Acid Sequence; D000818:Animals; D050260:Carbohydrate Metabolism / Q000502:physiology; D006031:Glycosylation; D006801:Humans; D037102:Lectins / Q000737:chemistry / Q000378:metabolism*; D008024:Ligands; D008562:Membrane Glycoproteins / Q000032:analysis / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D015202:Protein Engineering / Q000379:methods*; D054730:Protein Interaction Domains and Motifs; D040901:Proteomics / Q000379:methods*
D037102:Lectins; D008024:Ligands; D008562:Membrane Glycoproteins