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dc.contributor.authorAbu Saleh, Md
dc.contributor.authorSolayman, Md
dc.contributor.authorPaul, Sudip
dc.contributor.authorSaha, Moumoni
dc.contributor.authorKhalil, Md Ibrahim
dc.contributor.authorGan, Siew Hua
dc.date.accessioned2020-01-31T00:23:38Z
dc.date.available2020-01-31T00:23:38Z
dc.date.issued2016
dc.identifier.issn2314-6133
dc.identifier.doi10.1155/2016/9142190
dc.identifier.urihttp://hdl.handle.net/10072/391006
dc.description.abstractDespite the reported association of adiponectin receptor 1 (ADIPOR1) gene mutations with vulnerability to several human metabolic diseases, there is lack of computational analysis on the functional and structural impacts of single nucleotide polymorphisms (SNPs) of the human ADIPOR1 at protein level. Therefore, sequence-and structure-based computational tools were employed in this study to functionally and structurally characterize the coding nsSNPs of ADIPOR1 gene listed in the dbSNP database. Our in silico analysis by SIFT, nsSNPAnalyzer, PolyPhen-2, Fathmm, I-Mutant 2.0, SNPs&GO, PhD-SNP, PANTHER, and SNPeffect tools identified the nsSNPs with distorting functional impacts, namely, rs765425383 (A348G), rs752071352 (H341Y), rs759555652 (R324L), rs200326086 (L224F), and rs766267373 (L143P) from 74 nsSNPs of ADIPOR1 gene. Finally the aforementioned five deleterious nsSNPs were introduced using Swiss-PDB Viewer package within the X-ray crystal structure of ADIPOR1 protein, and changes in free energy for these mutations were computed. Although increased free energy was observed for all the mutants, the nsSNP H341Y caused the highest energy increase amongst all. RMSD and TM scores predicted that mutants were structurally similar to wild type protein. Our analyses suggested that the aforementioned variants especially H341Y could directly or indirectly destabilize the amino acid interactions and hydrogen bonding networks of ADIPOR1.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherHindawi Publishing
dc.relation.ispartofjournalBioMed Research International
dc.relation.ispartofvolume2016
dc.subject.fieldofresearchBiological sciences
dc.subject.fieldofresearchcode31
dc.subject.keywordsScience & Technology
dc.subject.keywordsLife Sciences & Biomedicine
dc.subject.keywordsBiotechnology & Applied Microbiology
dc.subject.keywordsMedicine, Research & Experimental
dc.subject.keywordsResearch & Experimental Medicine
dc.titleImpacts of Nonsynonymous Single Nucleotide Polymorphisms of Adiponectin Receptor 1 Gene on Corresponding Protein Stability: A Computational Approach
dc.typeJournal article
dc.type.descriptionC1 - Articles
dcterms.bibliographicCitationAbu Saleh, M; Solayman, M; Paul, S; Saha, M; Khalil, MI; Gan, SH, Impacts of Nonsynonymous Single Nucleotide Polymorphisms of Adiponectin Receptor 1 Gene on Corresponding Protein Stability: A Computational Approach, BioMed Research International, 2016, 2016
dcterms.dateAccepted2016-04-11
dcterms.licensehttp://creativecommons.org/licenses/by/4.0/
dc.date.updated2020-01-31T00:21:17Z
dc.description.versionVersion of Record (VoR)
gro.rights.copyright© 2016 Md. Abu Saleh et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
gro.hasfulltextFull Text
gro.griffith.authorSolayman, Md.


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