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Mutation goals in the vitamin D receptor predicted by computational methods

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dc.abstract.enThe mechanism through which nuclear receptors respond differentially to structurally distinct agonists is a poorly understood process. We present a computational method that identifies nuclear receptor amino acids that are likely involved in biological responses triggered by ligand binding. The method involves tracing how structural changes spread from the ligand binding pocket to the sites on the receptor surface, which makes it a good tool for studying allosteric effects. We employ the method to the vitamin D receptor and verify that the identified amino acids are biologically relevant using a broad range of experimental data and a genome browser. We infer that surface vitamin D receptor residues K141, R252, I260, T280, T287 and L417 are likely involved in cell differentiation and antiproliferation, whereas P122, D149, K321, E353 and Q385 are linked to carcinogenesis.
dc.affiliationUniwersytet Warszawski
dc.contributor.authorGront, Dominik
dc.contributor.authorSicińska, Wanda
dc.contributor.authorSiciński, Kamil
dc.date.accessioned2024-01-25T13:22:56Z
dc.date.available2024-01-25T13:22:56Z
dc.date.issued2018
dc.description.financeNie dotyczy
dc.description.volume183
dc.identifier.doi10.1016/J.JSBMB.2018.06.016
dc.identifier.issn0960-0760
dc.identifier.urihttps://repozytorium.uw.edu.pl//handle/item/113175
dc.languageeng
dc.pbn.affiliationchemical sciences
dc.relation.ispartofJournal of Steroid Biochemistry and Molecular Biology
dc.relation.pages210-220
dc.rightsClosedAccess
dc.sciencecloudnosend
dc.subject.enVitamin D receptor active sites
dc.subject.enVitamin D
dc.subject.enVitamin D analogs
dc.subject.enComputational analysis
dc.subject.enholoVDR crystal complexes
dc.titleMutation goals in the vitamin D receptor predicted by computational methods
dc.typeJournalArticle
dspace.entity.typePublication