Since many aspects of life are governed by interactions of proteins with other molecules, prediction of these interactions is of paramount importance. In the absence of an experimentally determined 3D structure for proteins interacting with other molecules, researchers may create a model for how they interact. It is possible to create models for complexes whose structures are unknown by using available experimental information of homologous structures. These models can assist in the understanding and guidance of experimental work. In this study, a combination of theoretical and experimental work is used to explore protein-carbohydrate interactions. A combination of homology modeling and docking experiments is used to predict and understand protein-carbohydrate interactions. Surface plasmon resonance is integrated to validate and quantify these interactions. Two applications are studied; the first is the salmon Rha binding lectin, SEL24K, and the second the discovery of a Man binding lectin, CUB domains, working in conjunction with a serine protease domain. These findings and modeling approaches can be used to explore and rationalize similar enzyme-lectin systems working on glycosylated environments, such as cell surfaces.
展开▼
