Please use this identifier to cite or link to this item: http://cmuir.cmu.ac.th/jspui/handle/6653943832/75654
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dc.contributor.authorSupat Jiranusornkulen_US
dc.contributor.authorPathomwat Wongrattanakamonen_US
dc.contributor.authorDarunee Hongwiseten_US
dc.contributor.authorSupachai Sakkhachornphopen_US
dc.contributor.authorChatchai Tayapiwatanaen_US
dc.date.accessioned2022-10-16T07:01:39Z-
dc.date.available2022-10-16T07:01:39Z-
dc.date.issued2021-06-01en_US
dc.identifier.issn15733904en_US
dc.identifier.issn15733149en_US
dc.identifier.other2-s2.0-85101032911en_US
dc.identifier.other10.1007/s10989-021-10175-2en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85101032911&origin=inwarden_US
dc.identifier.urihttp://cmuir.cmu.ac.th/jspui/handle/6653943832/75654-
dc.description.abstractIn eukaryotes, one of the most often noticed DNA-binding motifs are Cys2His2 zinc finger proteins which have been extensively utilized as a framework for designing novel DNA-binding proteins. In this study, the conformational change, and binding stability, affinity and interactions of the 2LTRZFP–HIV-1 2-LTR-circle junction complexes were successfully reproduced with MD simulations, MM-PBSA/GBSA and binding mode analyses. The binding free energies were obtained, and it was found that the calculated binding free energy of Zif1 is lower than Zif2 and together with pharmacophore modeling, these binding results indicate strong affinity of 2LTRZFP for the DNA. Mutants of 2LTRZFP were analyzed. The computed energies provided proof for a relationship between the binding free energy and total electrostatic interaction energy. The mutation in a key amino acid (Glu81Tyr) of the finger 3 in position 6 showed increased binding energy to the DNA. The result agrees with our previous study which showed that the HIV-1 IN may be hindered by the 2LTRZFP. The obtained results may assist in the design of ZFPs depended on the 2-LTR-circle junctions inhibition mechanism.en_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectChemical Engineeringen_US
dc.subjectChemistryen_US
dc.subjectPharmacology, Toxicology and Pharmaceuticsen_US
dc.titleMolecular Modeling for a Comparative Analysis of Interactions Between 2LTRZFP and 2-LTR-Circle Junctionsen_US
dc.typeJournalen_US
article.title.sourcetitleInternational Journal of Peptide Research and Therapeuticsen_US
article.volume27en_US
article.stream.affiliationsChiang Mai Universityen_US
Appears in Collections:CMUL: Journal Articles

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