Serpin–ligand interactions

• Published in: Methods (San Diego, Calif.) Calif.), 2004-02, Vol.32 (2), p.93-109
• Main Authors: Patston, Philip A, Church, Frank C, Olson, Steven T
• Format: Article
• Language: English
• Subjects: Binding Sites; Calorimetry; Chromatography, Affinity; Chromatography, Gel; Collodion - chemistry; Crystallography, X-Ray; Electrophoresis; Electrophoretic Mobility Shift Assay; Endopeptidases - metabolism; Gene Library; Genes, Reporter; Kinetics; Ligands; Protein Binding; Protein Conformation; Serpins - chemistry; Serpins - metabolism; Spectrum Analysis; Ultracentrifugation
• ISSN: 1046-2023; 1095-9130
• DOI: 10.1016/S1046-2023(03)00201-9

One of the more common features of serpins is the ability to bind various ligands. Ligand binding can occur so that the inhibitory properties of the serpin are regulated, so that the serpin can be localized, or to produce or modulate some other biological function of the serpin. Ligands known to affect serpin biologic activity include glycosaminoglycans such as heparin, heparan sulfate and dermatan sulfate, DNA, extracellular matrix proteins such as vitronectin and collagen, and small organic molecule hormones. Many different biochemical and biophysical techniques in conjunction with molecular biology and cell biology approaches have been used to study the binding of various ligands to serpins and to assess the influence of this binding on activity and structure. We summarize here the different approaches that have been used to identify serpin ligands and the many methods that have been used to characterize the interactions of these ligands with their cognate serpins.