SNP2Structure: A Public and Versatile Resource for Mapping and Three-Dimensional Modeling of Missense SNPs on Human Protein Structures

One of the long-standing challenges in biology is to understand how non-synonymous single nucleotide polymorphisms (nsSNPs) change protein structure and further affect their function. While it is impractical to solve all the mutated protein structures experimentally, it is quite feasible to model th...

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Main Authors: Difei Wang, Lei Song, Varun Singh, Shruti Rao, Lin An, Subha Madhavan
Format: Article
Language:English
Published: Elsevier 2015-01-01
Series:Computational and Structural Biotechnology Journal
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S2001037015000434
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spelling doaj-ce1b47a0f6ee4a26a7a442949942a3502020-11-24T21:02:24ZengElsevierComputational and Structural Biotechnology Journal2001-03702015-01-0113C51451910.1016/j.csbj.2015.09.002SNP2Structure: A Public and Versatile Resource for Mapping and Three-Dimensional Modeling of Missense SNPs on Human Protein StructuresDifei Wang0Lei Song1Varun Singh2Shruti Rao3Lin An4Subha Madhavan5Department of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University Medical Center, Washington, DC 20007, USAInnovation Center for Biomedical Informatics, Georgetown University Medical Center, Washington, DC 20007, USAInnovation Center for Biomedical Informatics, Georgetown University Medical Center, Washington, DC 20007, USAInnovation Center for Biomedical Informatics, Georgetown University Medical Center, Washington, DC 20007, USAInnovation Center for Biomedical Informatics, Georgetown University Medical Center, Washington, DC 20007, USADepartment of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University Medical Center, Washington, DC 20007, USAOne of the long-standing challenges in biology is to understand how non-synonymous single nucleotide polymorphisms (nsSNPs) change protein structure and further affect their function. While it is impractical to solve all the mutated protein structures experimentally, it is quite feasible to model the mutated structures in silico. Toward this goal, we built a publicly available structure database resource (SNP2Structure, https://apps.icbi.georgetown.edu/snp2structure) focusing on missense mutations, msSNP. Compared with web portals with similar aims, SNP2Structure has the following major advantages. First, our portal offers direct comparison of two related 3D structures. Second, the protein models include all interacting molecules in the original PDB structures, so users are able to determine regions of potential interaction changes when a protein mutation occurs. Third, the mutated structures are available to download locally for further structural and functional analysis. Fourth, we used Jsmol package to display the protein structure that has no system compatibility issue. SNP2Structure provides reliable, high quality mapping of nsSNPs to 3D protein structures enabling researchers to explore the likely functional impact of human disease-causing mutations.http://www.sciencedirect.com/science/article/pii/S2001037015000434Active site mutationsProtein structureMolecular modelingDisease causing SNPsSNP database
collection DOAJ
language English
format Article
sources DOAJ
author Difei Wang
Lei Song
Varun Singh
Shruti Rao
Lin An
Subha Madhavan
spellingShingle Difei Wang
Lei Song
Varun Singh
Shruti Rao
Lin An
Subha Madhavan
SNP2Structure: A Public and Versatile Resource for Mapping and Three-Dimensional Modeling of Missense SNPs on Human Protein Structures
Computational and Structural Biotechnology Journal
Active site mutations
Protein structure
Molecular modeling
Disease causing SNPs
SNP database
author_facet Difei Wang
Lei Song
Varun Singh
Shruti Rao
Lin An
Subha Madhavan
author_sort Difei Wang
title SNP2Structure: A Public and Versatile Resource for Mapping and Three-Dimensional Modeling of Missense SNPs on Human Protein Structures
title_short SNP2Structure: A Public and Versatile Resource for Mapping and Three-Dimensional Modeling of Missense SNPs on Human Protein Structures
title_full SNP2Structure: A Public and Versatile Resource for Mapping and Three-Dimensional Modeling of Missense SNPs on Human Protein Structures
title_fullStr SNP2Structure: A Public and Versatile Resource for Mapping and Three-Dimensional Modeling of Missense SNPs on Human Protein Structures
title_full_unstemmed SNP2Structure: A Public and Versatile Resource for Mapping and Three-Dimensional Modeling of Missense SNPs on Human Protein Structures
title_sort snp2structure: a public and versatile resource for mapping and three-dimensional modeling of missense snps on human protein structures
publisher Elsevier
series Computational and Structural Biotechnology Journal
issn 2001-0370
publishDate 2015-01-01
description One of the long-standing challenges in biology is to understand how non-synonymous single nucleotide polymorphisms (nsSNPs) change protein structure and further affect their function. While it is impractical to solve all the mutated protein structures experimentally, it is quite feasible to model the mutated structures in silico. Toward this goal, we built a publicly available structure database resource (SNP2Structure, https://apps.icbi.georgetown.edu/snp2structure) focusing on missense mutations, msSNP. Compared with web portals with similar aims, SNP2Structure has the following major advantages. First, our portal offers direct comparison of two related 3D structures. Second, the protein models include all interacting molecules in the original PDB structures, so users are able to determine regions of potential interaction changes when a protein mutation occurs. Third, the mutated structures are available to download locally for further structural and functional analysis. Fourth, we used Jsmol package to display the protein structure that has no system compatibility issue. SNP2Structure provides reliable, high quality mapping of nsSNPs to 3D protein structures enabling researchers to explore the likely functional impact of human disease-causing mutations.
topic Active site mutations
Protein structure
Molecular modeling
Disease causing SNPs
SNP database
url http://www.sciencedirect.com/science/article/pii/S2001037015000434
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