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Effects of Disease-Associated Mutations and SNP on Protein Structures

Recently, information on mutations associated with disease and SNP (Single Nucleotide Polymorphism) has been rapidly increasing. Many of these mutations are thought to affect the structure and interactions of proteins through amino-acid substitutions. Therefore, it is important to assess the effect of these mutations on the structure and interactions of proteins, in order to understand the molecular mechanism of disease. We have been collecting mutations associated with human diseases, and integrated the information into 3DinSight, an integrated database for sequence, structure, property and function of biomolecules [1]. We have mapped the mutations on protein structures and visualized the location with direct link to the disease information. In this study, we analyze the effect of these mutations on the structure and physical and functional properties of protein in a systematic way. In order to highlight the effect, we also compared the result from a similar analysis of dbSNP [2]. Based on these analyses, we attempt to establish the relationship between the disease-related mutations and structural properties of proteins.