Functional and Structural Features of Disease-Related Protein Variants.

disease-related Pfam domains disease-related protein variations disease-related reactome pathways genetic variations polar solvent accessible surface protein structure

Journal

International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791

Informations de publication

Date de publication:
27 Mar 2019
Historique:
received: 08 02 2019
revised: 22 03 2019
accepted: 22 03 2019
entrez: 3 4 2019
pubmed: 3 4 2019
medline: 17 7 2019
Statut: epublish

Résumé

Modern sequencing technologies provide an unprecedented amount of data of single-nucleotide variations occurring in coding regions and leading to changes in the expressed protein sequences. A significant fraction of these single-residue variations is linked to disease onset and collected in public databases. In recent years, many scientific studies have been focusing on the dissection of salient features of disease-related variations from different perspectives. In this work, we complement previous analyses by updating a dataset of disease-related variations occurring in proteins with 3D structure. Within this dataset, we describe functional and structural features that can be of interest for characterizing disease-related variations, including major chemico-physical properties, the strength of association to disease of variation types, their effect on protein stability, their location on the protein structure, and their distribution in Pfam structural/functional protein models. Our results support previous findings obtained in different data sets and introduce Pfam models as possible fingerprints of patterns of disease related single-nucleotide variations.

Identifiants

pubmed: 30934684
pii: ijms20071530
doi: 10.3390/ijms20071530
pmc: PMC6479756
pii:
doi:

Substances chimiques

Mutant Proteins 0
Solvents 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Références

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Auteurs

Castrense Savojardo (C)

Biocomputing Group, Department of Pharmacy and Biotechnology, University of Bologna, 40126 Bologna, Italy. castrense.savojardo2@unibo.it.

Giulia Babbi (G)

Biocomputing Group, Department of Pharmacy and Biotechnology, University of Bologna, 40126 Bologna, Italy. giulia.babbi3@unibo.it.

Pier Luigi Martelli (PL)

Biocomputing Group, Department of Pharmacy and Biotechnology, University of Bologna, 40126 Bologna, Italy. pierluigi.martelli@unibo.it.

Rita Casadio (R)

Biocomputing Group, Department of Pharmacy and Biotechnology, University of Bologna, 40126 Bologna, Italy. rita.casadio@unibo.it.
Institute of Biomembranes, Bioenergetics and Molecular Biotechnologies (IBIOM), Italian National Research Council (CNR), 70126 Bari, Italy. rita.casadio@unibo.it.

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Classifications MeSH