Repository logo
 

Prediction by graph theoretic measures of structural effects in proteins arising from non-synonymous single nucleotide polymorphisms.

Published version
Peer-reviewed

Type

Article

Change log

Authors

Cheng, Tammy MK 
Lu, Yu-En 
Vendruscolo, Michele  ORCID logo  https://orcid.org/0000-0002-3616-1610
Lio', Pietro 
Blundell, Tom L 

Abstract

Recent analyses of human genome sequences have given rise to impressive advances in identifying non-synonymous single nucleotide polymorphisms (nsSNPs). By contrast, the annotation of nsSNPs and their links to diseases are progressing at a much slower pace. Many of the current approaches to analysing disease-associated nsSNPs use primarily sequence and evolutionary information, while structural information is relatively less exploited. In order to explore the potential of such information, we developed a structure-based approach, Bongo (Bonds ON Graph), to predict structural effects of nsSNPs. Bongo considers protein structures as residue-residue interaction networks and applies graph theoretical measures to identify the residues that are critical for maintaining structural stability by assessing the consequences on the interaction network of single point mutations. Our results show that Bongo is able to identify mutations that cause both local and global structural effects, with a remarkably low false positive rate. Application of the Bongo method to the prediction of 506 disease-associated nsSNPs resulted in a performance (positive predictive value, PPV, 78.5%) similar to that of PolyPhen (PPV, 77.2%) and PANTHER (PPV, 72.2%). As the Bongo method is solely structure-based, our results indicate that the structural changes resulting from nsSNPs are closely associated to their pathological consequences.

Description

Keywords

Artificial Intelligence, Computational Biology, DNA Mutational Analysis, Genetic Predisposition to Disease, Humans, Models, Genetic, Models, Molecular, Neural Networks, Computer, Polymorphism, Single Nucleotide, Predictive Value of Tests, Protein Conformation, Protein Interaction Mapping, Proteins, Sequence Alignment, Sequence Analysis, Protein, Thermodynamics

Journal Title

PLoS Comput Biol

Conference Name

Journal ISSN

1553-734X
1553-7358

Volume Title

4

Publisher

Public Library of Science (PLoS)