Abstract
Almost all (99.9%) nucleotide bases are exactly the same in all people, however, the remaining 0.1% account for about 1.4 million locations where single-base DNA differences/polymorphisms (SNPs) occur in humans. Some of these SNPs, called non-synonymous SNPs (nsSNPs), result in a change of the amino acid sequences of the corresponding proteins affecting protein functions and interactions. This review summarizes the plausible mechanisms that nsSNPs may affect the normal cellular function. It outlines the approaches that have been developed in the past to predict the effects caused by nsSNPs with special emphasis on the methods that use structural information. The review provides systematic information on the available resources for predicting the effects of nsSNPs and includes a comprehensive list of existing SNP databases and their features. While nsSNPs resulting in amino acid substitution in the core of a protein may affect protein stability irreversibly, the effect of an nsSNP resulting to a mutation at the surface of a protein or at the interface of protein-protein complexes, could, in principle be, subject of drug therapy. The importance of understanding the effects caused by nsSNP mutations at the protein-protein and protein-DNA interfaces is outlined.
Keywords: nsSNP, residue mutation, disease-causing SNP, protein-protein interactions, protein stability
Current Pharmaceutical Biotechnology
Title: Approaches and Resources for Prediction of the Effects of Non-Synonymous Single Nucleotide Polymorphism on Protein Function and Interactions
Volume: 9 Issue: 2
Author(s): S. Teng, E. Michonova-Alexova and E. Alexov
Affiliation:
Keywords: nsSNP, residue mutation, disease-causing SNP, protein-protein interactions, protein stability
Abstract: Almost all (99.9%) nucleotide bases are exactly the same in all people, however, the remaining 0.1% account for about 1.4 million locations where single-base DNA differences/polymorphisms (SNPs) occur in humans. Some of these SNPs, called non-synonymous SNPs (nsSNPs), result in a change of the amino acid sequences of the corresponding proteins affecting protein functions and interactions. This review summarizes the plausible mechanisms that nsSNPs may affect the normal cellular function. It outlines the approaches that have been developed in the past to predict the effects caused by nsSNPs with special emphasis on the methods that use structural information. The review provides systematic information on the available resources for predicting the effects of nsSNPs and includes a comprehensive list of existing SNP databases and their features. While nsSNPs resulting in amino acid substitution in the core of a protein may affect protein stability irreversibly, the effect of an nsSNP resulting to a mutation at the surface of a protein or at the interface of protein-protein complexes, could, in principle be, subject of drug therapy. The importance of understanding the effects caused by nsSNP mutations at the protein-protein and protein-DNA interfaces is outlined.
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Cite this article as:
Teng S., Michonova-Alexova E. and Alexov E., Approaches and Resources for Prediction of the Effects of Non-Synonymous Single Nucleotide Polymorphism on Protein Function and Interactions, Current Pharmaceutical Biotechnology 2008; 9 (2) . https://dx.doi.org/10.2174/138920108783955164
DOI https://dx.doi.org/10.2174/138920108783955164 |
Print ISSN 1389-2010 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4316 |
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