<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Knappenberger AJ</submitter><funding>U.S. Department of Health and Human Services</funding><funding>NIGMS NIH HHS</funding><pagination>1361-1366</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7311191</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>59(13)</volume><pubmed_abstract>The modularity of protein domains is well-known, but the existence of independent domains that confer function in RNA is less established. Recently, a family of RNA aptamers termed &lt;i>ykkC&lt;/i> was discovered; they bind at least four ligands of very different chemical composition, including guanidine, phosphoribosyl pyrophosphate (PRPP), and guanosine tetraphosphate (ppGpp) (graphical abstract). Structures of these aptamers revealed an architecture characterized by two coaxial helical stacks. The first helix appears to be a generic scaffold, while the second helix forms the most contacts to the ligands. To determine if these two regions within the aptamer are modular units for ligand recognition, we swapped the ligand-binding coaxial stacks of a guanidine aptamer and a PRPP aptamer. This op</pubmed_abstract><journal>Biochemistry</journal><pubmed_title>A Modular RNA Domain That Confers Differential Ligand Specificity.</pubmed_title><pmcid>PMC7311191</pmcid><funding_grant_id>P01 GM022778</funding_grant_id><funding_grant_id>GM022778</funding_grant_id><funding_grant_id>T32 GM100884</funding_grant_id><pubmed_authors>Focht CM</pubmed_authors><pubmed_authors>Strobel SA</pubmed_authors><pubmed_authors>Reiss CW</pubmed_authors><pubmed_authors>Knappenberger AJ</pubmed_authors></additional><is_claimable>false</is_claimable><name>A Modular RNA Domain That Confers Differential Ligand Specificity.</name><description>The modularity of protein domains is well-known, but the existence of independent domains that confer function in RNA is less established. Recently, a family of RNA aptamers termed &lt;i>ykkC&lt;/i> was discovered; they bind at least four ligands of very different chemical composition, including guanidine, phosphoribosyl pyrophosphate (PRPP), and guanosine tetraphosphate (ppGpp) (graphical abstract). Structures of these aptamers revealed an architecture characterized by two coaxial helical stacks. The first helix appears to be a generic scaffold, while the second helix forms the most contacts to the ligands. To determine if these two regions within the aptamer are modular units for ligand recognition, we swapped the ligand-binding coaxial stacks of a guanidine aptamer and a PRPP aptamer. This op</description><dates><release>2020-01-01T00:00:00Z</release><publication>2020 Apr</publication><modification>2026-04-29T00:17:24.53Z</modification><creation>2022-02-09T12:46:07.826Z</creation></dates><accession>S-EPMC7311191</accession><cross_references><pubmed>32202416</pubmed><doi>10.1021/acs.biochem.0c00117</doi></cross_references></HashMap>