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Please use this identifier to cite or link to this item: http://repository.iitr.ac.in/handle/123456789/19244
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dc.contributor.authorJoshi N.-
dc.contributor.authorNagar N.-
dc.contributor.authorGulati K.-
dc.contributor.authorGangele K.-
dc.contributor.authorMishra A.-
dc.contributor.authorKumar D.-
dc.contributor.authorPoluri, Krishna Mohan-
dc.date.accessioned2022-01-31T08:27:47Z-
dc.date.available2022-01-31T08:27:47Z-
dc.date.issued2020-
dc.identifier.citationInternational Journal of Biological Macromolecules(2020), 156(): 239-251-
dc.identifier.issn1418130-
dc.identifier.other32289428-
dc.identifier.urihttps://doi.org/10.1016/j.ijbiomac.2020.04.067-
dc.identifier.urihttp://repository.iitr.ac.in/handle/123456789/19244-
dc.description.abstractChemokines are a sub-group of cytokines that regulate the leukocyte migration. Monocyte chemoattractant protein-1 (MCP/CCL2) is one of the essential CC chemokine that regulates the migration of monocytes into inflamed tissues. It has been observed that the primary sequences of CCL2 orthologs among rodents and primates vary significantly at the C-terminal region. However, no structural details are available for the rodentia family CCL2 proteins. The current study unravelled the structural, dynamics and in-silico functional characteristics of murine CCL2 chemokine using a comprehensive set of NMR spectroscopy techniques and evolutionary approaches. The study unravelled that the N-terminal portion of the murine CCL2 forms a canonical CC chemokine dimer similar to that of human CCL2. However, unlike human CCL2, the murine ortholog exhibits extensive dynamics in the μs-ms timescales. The presence of C-terminal region of the murine CCL2 protein/rodentia family is highly glycosylated, completely disordered, and inhibits the folding of the structured CCL2 regions. Further, it has been observed that the glycosaminoglycan binding surfaces of these orthologs proteins are greatly differed. In a nut shell, this comparative study provided the role of molecular evolution in generating orthologous proteins with differential structural and dynamics characteristics to engage them in specific molecular interactions.-
dc.language.isoen_US-
dc.publisherElsevier B.V.-
dc.relation.ispartofInternational Journal of Biological Macromolecules-
dc.subjectChemokines-
dc.subjectG-protein coupled receptor (GPCR)-
dc.subjectGlycosaminoglycans (GAGs)-
dc.subjectMolecular evolution-
dc.subjectNuclear magnetic resonance (NMR)-
dc.subjectdimer-
dc.subjectglycosaminoglycan-
dc.subjectmonocyte chemotactic protein 1-
dc.subjectamino acid sequence-
dc.subjectamino terminal sequence-
dc.subjectanimal cell-
dc.subjectArticle-
dc.subjectbiophysics-
dc.subjectcarboxy terminal sequence-
dc.subjectcomparative study-
dc.subjectcomputer model-
dc.subjectcontrolled study-
dc.subjectdimerization-
dc.subjectdissociati-
dc.titleDissecting the differential structural and dynamics features of CCL2 chemokine orthologs-
dc.typeArticle-
dc.scopusid57194069482-
dc.scopusid57216362264-
dc.scopusid56998446900-
dc.scopusid57191832383-
dc.scopusid57214220793-
dc.scopusid57202477914-
dc.scopusid55842079400-
dc.affiliationJoshi, N., Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand 247667, India-
dc.affiliationNagar, N., Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand 247667, India-
dc.affiliationGulati, K., Departm-
dc.description.fundingDepartment of Biotechnology, Ministry of Science and Technology, India, DBT: BT/07/IYBA/2013-19 Jacobs Research Funds, JRF University Grants Committee, UGC Department of Science and Technology, Ministry of Science and Technology, India, DST.KMP acknowledge the receipt of Grants CRG/2018/001329 and SERB-SB/YS/LS-380/2013 from SERB - DST , and DBT -IYBA fellowship – BT/07/IYBA/2013-19 . NJ acknowledge the receipt of JRF & SRF fellowship from UGC. Authors acknowledge the support of biophysica.-
dc.description.correspondingauthorPoluri, K.M.; Department of Biotechnology, India; email: krishfbt@iitr.ac.in-
Appears in Collections:Journal Publications [BT]

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