Narrow Results

Carbohydrates are considered the molecules of molecular recognition because of their influential roles in interacting with viruses, toxins and cell–cell adhesion phenomena. The recognition phenomena are due to the diversified sequences and three-dimensional structures of carbohydrates and their conformational dynamics, binding site residues of proteins and noncovalent interactions between them. This review provides (1) different databases of carbohydrates, which have vital roles in studying protein–carbohydrate interactions, (2) the role of molecular dynamics (MD) simulations for deducing conformational models of carbohydrates as well as studying the interactions between proteins and carbohydrates and (3) design of inhibitors to avoid pathogenic interactions.

Carbohydrates are known as sugars or saccharides, which range from simple sugars (glucose) to complex polysaccharides (cellulose). Proteins that interact with carbohydrates are called carbohydrate-binding proteins, and the interaction between proteins and carbohydrates is important for several biological processes, such as cell–cell adhesion, immune response, pathogen recognition, and enzyme catalysis. Mutations in these proteins may impact their structure, binding affinity and function, and understanding the mutational effects on protein–carbohydrate interactions is essential for elucidating their molecular mechanisms. In this chapter, we provide a comprehensive overview of (i) databases available for binding affinity of protein–carbohydrate complexes and their mutants, (ii) analysis and prediction of mutational effects on binding affinity of protein–carbohydrate complexes, (iii) effects of mutation at the interaction sites based on diseases, and (iv) potential applications. The information provided in this chapter will provide insights to understand mutational effects on binding affinity and disease-causing mutations in protein–carbohydrate complexes and design therapeutic strategies.