Single residue mutations in proteins are known to affect protein stability and function. As a consequence, they can be disease associated. Available computational methods starting from protein sequence/structure can predict whether a mutated residue is or not disease associated and whether it is pro
The SAAPdb web resource: A large-scale structural analysis of mutant proteins
β Scribed by Jacob M. Hurst; Lisa E.M. McMillan; Craig T. Porter; James Allen; Adebola Fakorede; Andrew C.R. Martin
- Publisher
- John Wiley and Sons
- Year
- 2009
- Tongue
- English
- Weight
- 182 KB
- Volume
- 30
- Category
- Article
- ISSN
- 1059-7794
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β¦ Synopsis
The Single Amino Acid Polymorphism database (SAAPdb) is a new resource for the analysis and visualization of the structural effects of mutations. Our analytical approach is to map single nucleotide polymorphisms (SNPs) and pathogenic deviations (PDs) to protein structural data held within the Protein Data Bank. By mapping mutations onto protein structures, we can hypothesize whether the mutant residues will have any local structural effect that may "explain" a deleterious phenotype. Our prior work used a similar approach to analyze mutations within a single protein. An analysis of the contents of SAAPdb indicates that there are clear differences in the sequence and structural characteristics of SNPs and PDs, and that PDs are more often explained by our structural analysis. This mapping and analysis is a useful resource for the mutation community and is publicly available at http://www.bioinf.org.uk/saap/db/.
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