title: Structures of glycans bound to receptors from saturation transfer difference (STD) NMR spectroscopy: quantitative analysis by using CORCEMA-ST.
abstract: Glycan-receptor interactions are of fundamental relevance for a large number of biological processes, and their kinetics properties (medium/weak binding affinities) make them appropriated to be studied by ligand observed NMR techniques, among which saturation transfer difference (STD) NMR spectroscopy has been shown to be a very robust and powerful approach. The quantitative analysis of the results from a STD NMR study of a glycan-receptor interaction is essential to be able to translate the resulting spectral intensities into a 3D molecular model of the complex. This chapter describes how to carry out such a quantitative analysis by means of the Complete Relaxation and Conformational Exchange Matrix Approach for STD NMR (CORCEMA-ST), in general terms, and an example of a previous work on an antibody-glycan interaction is also shown.
authors.affiliation: Andalusian Centre for Nanomedicine and Biotechnology (BIONAND), C/Severo Ochoa 35, Parque Tecnológico de Andalucía, 29590, Campanillas, Málaga, Spain.
authors.forename: Pedro M
authors.initials: PM
authors.lastname: Enríquez-Navas
authors.forename: Cinzia
authors.initials: C
authors.lastname: Guzzi
authors.forename: Juan C
authors.initials: JC
authors.lastname: Muñoz-García
authors.forename: Pedro M
authors.initials: PM
authors.lastname: Nieto
authors.forename: Jesús
authors.initials: J
authors.lastname: Angulo
mesh_terms: D002236:Carbohydrate Conformation; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008958:Models, Molecular; D011134:Polysaccharides / Q000737:chemistry* / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000378:metabolism*; D012984:Software
chemical_list: D011134:Polysaccharides; D011956:Receptors, Cell Surface