Show simple item record

dc.contributor.authorSolayman, Md
dc.contributor.authorAbu Saleh, Md
dc.contributor.authorPaul, Sudip
dc.contributor.authorKhalil, Md Ibrahim
dc.contributor.authorGan, Siew Hua
dc.date.accessioned2021-09-16T00:54:29Z
dc.date.available2021-09-16T00:54:29Z
dc.date.issued2017
dc.identifier.issn1476-9271
dc.identifier.doi10.1016/j.compbiolchem.2017.03.005
dc.identifier.urihttp://hdl.handle.net/10072/408019
dc.description.abstractPolymorphisms of the ADIPOR2 gene are frequently linked to a higher risk of developing diseases including obesity, type 2 diabetes and cardiovascular diseases. Though mutations of the ADIPOR2 gene are detrimental, there is a lack of comprehensive in silico analyses of the functional and structural impacts at the protein level. Considering the involvement of ADIPOR2 in glucose uptake and fatty acid oxidation, an in silico functional analysis was conducted to explore the possible association between genetic mutations and phenotypic variations. A genomic analysis of 82 nonsynonymous SNPs in ADIPOR2 was initiated using SIFT followed by the SNAP2, nsSNPAnalyzer, PolyPhen-2, SNPs&GO, FATHMM and PROVEAN servers. A total of 10 mutations (R126W, L160Q, L195P, F201S, L235R, L235P, L256R, Y328H, E334K and Q349H) were predicted to have deleterious effects on the ADIPOR2 protein and were therefore selected for further analysis. Theoretical models of the variants were generated by comparative modeling via MODELLER 9.16. A protein structural analysis of these amino acid variants was performed using SNPeffect, I-Mutant, ConSurf, Swiss-PDB Viewer and NetSurfP to explore their solvent accessibility, molecular dynamics and energy minimization calculations. In addition, FTSite was used to predict the ligand binding sites, while NetGlycate, NetPhos2.0, UbPerd and SUMOplot were used to predict post-translational modification sites. All of the variants showed increased free energy, though F201S exhibited the highest energy increase. The root mean square deviation values of the modeled mutants strongly indicated likely pathogenicity. Remarkably, three binding sites were detected on ADIPOR2, and two mutations at positions 328 and 201 were found in the first and second binding pockets, respectively. Interestingly, no mutations were found at the post-translational modification sites. These genetic variants can provide a better understanding of the wide range of disease susceptibility associated with ADIPOR2 and aid the development of new molecular diagnostic markers for these diseases. The findings may also facilitate the development of novel therapeutic elements for associated diseases.
dc.description.peerreviewedYes
dc.languageEnglish
dc.publisherElsevier
dc.relation.ispartofpagefrom175
dc.relation.ispartofpageto185
dc.relation.ispartofjournalComputational Biology and Chemistry
dc.relation.ispartofvolume68
dc.subject.fieldofresearchChemical sciences
dc.subject.fieldofresearchBiological sciences
dc.subject.fieldofresearchcode34
dc.subject.fieldofresearchcode31
dc.subject.keywordsScience & Technology
dc.subject.keywordsLife Sciences & Biomedicine
dc.subject.keywordsTechnology
dc.subject.keywordsBiology
dc.subject.keywordsComputer Science, Interdisciplinary Applications
dc.titleIn silico analysis of nonsynonymous single nucleotide polymorphisms of the human adiponectin receptor 2 (ADIPOR2) gene
dc.typeJournal article
dc.type.descriptionC1 - Articles
dcterms.bibliographicCitationSolayman, M; Abu Saleh, M; Paul, S; Khalil, MI; Gan, SH, In silico analysis of nonsynonymous single nucleotide polymorphisms of the human adiponectin receptor 2 (ADIPOR2) gene, Computational Biology and Chemistry, 2017, 68, pp. 175-185
dcterms.dateAccepted2017-03-06
dc.date.updated2021-09-16T00:52:47Z
gro.hasfulltextNo Full Text
gro.griffith.authorSolayman, Md.


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

  • Journal articles
    Contains articles published by Griffith authors in scholarly journals.

Show simple item record