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A structural perspective of RNA recognition by intrinsically disordered proteins

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dc.contributor.author Basu, Sushmita
dc.date.accessioned 2026-01-13T09:32:37Z
dc.date.available 2026-01-13T09:32:37Z
dc.date.issued 2016-05
dc.identifier.uri https://link.springer.com/article/10.1007/s00018-016-2283-1
dc.identifier.uri http://dspace.bits-pilani.ac.in:8080/jspui/handle/123456789/20533
dc.description.abstract Protein-RNA recognition is essential for gene expression and its regulation, which is indispensable for the survival of the living organism at one hand, on the other hand, misregulation of this recognition may lead to their extinction. Polymorphic conformation of both the interacting partners is a characteristic feature of such molecular recognition that promotes the assembly. Many RNA binding proteins (RBP) or regions in them are found to be intrinsically disordered, and this property helps them to play a central role in the regulatory processes. Sequence composition and the length of the flexible linkers between RNA binding domains in RBPs are crucial in making significant contacts with its partner RNA. Polymorphic conformations of RBPs can provide thermodynamic advantage to its binding partner while acting as a chaperone. Prolonged extensions of the disordered regions in RBPs also contribute to the stability of the large cellular machines including ribosome and viral assemblies. The involvement of these disordered regions in most of the significant cellular processes makes RBPs highly associated with various human diseases that arise due to their misregulation. en_US
dc.language.iso en en_US
dc.publisher Springer en_US
dc.subject Biology en_US
dc.subject Protein–RNA interactions en_US
dc.subject RNA-binding proteins en_US
dc.subject Intrinsic disorder en_US
dc.subject Gene regulation en_US
dc.title A structural perspective of RNA recognition by intrinsically disordered proteins en_US
dc.type Article en_US


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